Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.R900037199 on May 4, 2000

J. Biol. Chem., Vol. 275, Issue 30, 22607-22610, July 28, 2000
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/30/22607    most recent
R900037199v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Calderwood, D. A.
Right arrow Articles by Ginsberg, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Calderwood, D. A.
Right arrow Articles by Ginsberg, M. H.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

MINIREVIEW
Integrins and Actin Filaments: Reciprocal Regulation of Cell Adhesion and Signaling*

David A. CalderwoodDagger , Sanford J. ShattilDagger §, and Mark H. GinsbergDagger

From the Dagger  Department of Vascular Biology and § Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037

    INTRODUCTION
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

Integrin adhesion receptors link the extracellular matrix (ECM)1 to the actin cytoskeleton and transmit biochemical signals and mechanical force across the plasma membrane. This enables cells to generate traction during migration and exert tension during matrix remodeling (1). Cytoskeletal linkages also enable integrins to mediate cell adhesion and regulate cell shape and gene expression (1). Here we will summarize the evidence for direct interactions between integrin cytoplasmic tails and specific actin-binding proteins and discuss how these interactions influence cell adhesion, cell spreading, and migration.

    Role of Integrin Cytoplasmic Tails in Integrin-Cytoskeleton Linkages
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

Integrin alpha  and beta  subunits are type I transmembrane proteins expressed in surface membranes as heterodimers. Each consists of a large extracellular domain, a single transmembrane segment, and a relatively short cytoplasmic tail. The latter contains anywhere from 20 to 70 amino acid residues, with the notable exception of the much larger beta 4 tail, which is linked primarily to intermediate filaments instead of actin filaments (2). beta -Cytoplasmic tails are necessary and sufficient to link integrins to the actin cytoskeleton (2). In contrast, there is less evidence to date that alpha  tails are directly linked to the cytoskeleton; indeed the removal of the alpha 1, alpha 4, or alpha IIb cytoplasmic tail appears to increase beta  tail-mediated interactions with the cytoskeleton (2). Direct binding of the signaling adapter protein paxillin to alpha 4 cytoplasmic tails has recently been demonstrated, and this binding regulates alpha 4beta 1-mediated cell spreading, migration, and stress fiber formation (3). There is direct biochemical support for the interaction of alpha  and beta  tails with each other (4, 5) and for the modulation of this interaction by the binding of ligands to the extracellular domain (6). Consequently, regulated changes in the interactions between the alpha  and beta  tails may affect integrin-cytoskeleton linkages.

In addition to mediating integrin linkages with the actin cytoskeleton, beta  cytoplasmic tails are important for adhesion, spreading, and migration of cells on ECM, processes dependent on an intact actin cytoskeleton. Integrins typically cluster within "matrix adhesions," sites of close apposition of the cell membrane to the ECM. Matrix adhesions are extremely dynamic and heterogeneous structures with respect to size, composition, and orientation to actin filaments (7, 9). The largest ones are usually referred to as focal adhesions (FA), which are aligned at the ends of actin stress fibers (2, 8, 9). As such, FA represent a morphologically prominent association between integrins and the cytoskeleton, and investigation of integrin targeting to FA has shed light on the mechanisms of integrin-cytoskeleton association.

Mutational analysis of the 47-amino acid beta 1 cytoplasmic tail has identified three clusters of amino acids important for integrin localization to FA, a membrane-proximal region and two conserved NPXY (single-letter amino acid code) motifs (10). Similar motifs in the beta 3 cytoplasmic tail are important for localization of beta 3 integrins to FA (11). An additional Thr-containing motif between the two NPXY sites has also been implicated in beta 2 integrin-cytoskeleton linkages (12).

    Specific Integrin-Cytoskeleton Linkages
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

Integrins are linked to actin filaments by specific actin-binding proteins, and there is now an emerging consensus concerning which proteins are involved (Fig. 1).


View larger version (23K):
[in this window]
[in a new window]
 
Fig. 1.   Models of the physical links between integrins and F-actin. When known, the modular architecture of the linking proteins is shown based on domain assignments by the SMART program (13). The beta  integrin tail is depicted binding to ERM domains within the talin head domain; however, integrin-binding sites have also been identified in the rod domain. The spectrin repeats within the alpha -actinin rod domain mediate binding to the integrin beta  tail; however, it is not known which of the three repeats contains the binding site. Filamin binds integrins via C-terminal filamin repeats; however, the exact binding site has not yet been determined.

Talin-mediated Linkages-- Talin is composed of two ~270-kDa subunits arranged as an anti-parallel homodimer (8), and it co-localizes with integrins at certain sites of cell-substratum contact. Talin is a major structural component of FA along with actin and vinculin. It consists of an N-terminal ~50-kDa globular head domain, which includes an ~200-amino acid region with homology to the ezrin, radixin, and moesin (ERM) family of proteins, and an ~220-kDa, C-terminal rod domain containing a conserved ILWEQ actin-binding domain (8, 13). Talin contains binding sites for actin, vinculin, focal adhesion kinase, phospholipids, and the transmembrane protein laylin (8, 14). Talin was the first actin-binding protein shown to directly bind integrins and was proposed to mediate the link to the actin cytoskeleton (2). Talin binds to beta 1, beta 2, and beta 3 and more weakly to beta 7 integrin cytoplasmic tails (15-18). Talin accumulation is an early step in FA formation and requires integrins but not vinculin (19). Microinjection of antibodies to talin or talin antisense RNA disrupts stress fibers and inhibits adhesion, spreading, and migration of fibroblasts and HeLa cells (8, 20).

The significance of talin for integrin function has been underscored by studies of talin-null ES cells, which exhibit extensive membrane blebbing, defects in cell adhesion and spreading, and a failure to assemble FA or stress fibers (21). These results suggest that talin is required for the integrin-cytoskeleton associations needed for FA and stress fiber formation. However, undifferentiated talin-null ES cells also express reduced levels of beta 1 integrin, vinculin, and alpha -actinin, which may contribute to the phenotype. Following differentiation of talin-null ES cells, only two morphologically distinct cell types emerged, and no organized tissues were formed (21). The differentiated cells expressed normal levels of beta 1 integrin and vinculin and were capable of spreading and forming actin filaments and FA-like structures, indicating that in a subset of differentiated cell types, intact talin is dispensable for maintenance of beta 1 integrin expression and FA assembly.

Integrin-binding sites have been localized to both the talin-head and rod domains (17, 18), suggesting that binding of two or more integrin beta  tails to the talin dimer may facilitate integrin clustering (Fig. 1). Binding of both the head and rod domains are inhibited by Tyr to Ala mutations in the membrane-proximal NPXY motif of beta 1 and beta 3 integrins (15, 17, 22), consistent with the failure of integrins expressing this mutation to localize to FA (10, 11). In v-Src-transformed cells, which exhibit reduced cell adhesion and a disorganized cytoskeleton, the NPXY motif in the beta 1 tail is phosphorylated on tyrosine, and talin binding is inhibited (23). Furthermore, synthetic peptides spanning the NPXY motif bind purified talin and inhibit talin binding to beta 1 (22, 23). Thus, the talin-binding site in the beta 1 tail includes this sequence.

However, other regions of the beta  tail are likely to contribute to the interaction with talin because the NPXY motif is highly conserved between integrin beta  subunits, but talin displays differential binding to various integrin beta  tails (15). Indeed, deletion of the C-terminal 13 amino acids of the beta 1 cytoplasmic tail, which leaves the membrane-proximal NPXY site intact, inhibits both talin binding in vitro and co-localization of talin and actin with clustered beta 1 integrins in vivo (22, 24). In contrast, deletion of only the four most C-terminal amino acids from beta 1 has no effect on talin binding or recruitment of talin and actin to sites of clustered integrins (22, 24). Furthermore, a recent report concluded that talin could bind specifically to peptides corresponding to the membrane-proximal sequence of the beta 3 tail (18). Thus, further work is required to determine the precise mode of interaction between integrin beta  tails and talin.

Filamin-mediated Linkages-- Three distinct filamin genes have been reported, and alternative splicing allows for additional isoforms (25). Filamins are actin filament cross-linking proteins composed of two parallel 280-kDa subunits. Each subunit contains an N-terminal actin-binding domain composed of two calponin homology domains, followed by 23 repeating domains (8, 13). Depending on the filamin:F-actin ratio, filamin reinforces loose microfilament nets such as those found in the cell cortex (Fig. 1) or tightly packed bundles as found in stress fibers (8). Filamin also binds to the cytoplasmic domains of transmembrane proteins (e.g. GP Ibalpha ) and to intracellular signaling molecules (e.g. RalA) (25, 26). Filamin localizes to the cortical actin cytoskeleton and along the length of stress fibers but is also found in some FA (8).

beta 1A, beta 2, beta 3, beta 7, and to a lesser extent beta 1D integrin tails can bind filamin, and Tyr to Ala point mutations in the membrane-proximal beta 1 NPXY motif inhibit binding (15, 27). Both filamin and F-actin are recruited to beta 1-containing FA in response to mechanical stress, but F-actin recruitment does not take place in melanoma cells lacking filamin (28). The gene encoding human filamin-1 is located on the X chromosome, and mutations of this gene are associated with periventricular heterotopia, indicating a requirement for filamin-1 in neuronal migration during brain development (26). Loss of filamin-1 expression in neuronal or melanocytic cells results in impaired migration and altered morphology (26, 29). However, filamin-1 null melanocytic cells also have reduced levels of many cell surface receptors, including beta  integrins (30), which may account for some of these phenotypes.

alpha -Actinin-mediated Linkages-- alpha -Actinin is another homodimeric actin-binding protein localized to FA (8). Non-muscle alpha -actinin monomers are ~100-kDa rodlike proteins containing three functional domains: an N-terminal actin-binding domain composed of two calponin homology domains, a central region of four spectrin-like repeats, and a C-terminal domain containing two EF hands. At least two alpha -actinin genes and alternative splicing allow for production of a number of alpha -actinin isoforms. In addition to binding F-actin, alpha -actinin binds the FA proteins vinculin, zyxin, and beta 1, beta 2, and beta 3 integrins (2, 8) (Figs. 1 and 2). alpha -Actinin targets to FA in microinjected cells and in a cell-free system, apparently by interaction with beta  cytoplasmic tails (31, 32). The binding sites for alpha -actinin have been localized to the membrane-proximal half of the beta 1 or beta 2 integrin tail, and binding to beta 2 is negatively regulated by sequences in the C-terminal region of the tail (16). The membrane-proximal location of the alpha -actinin-binding site within beta  tails is consistent with the observation that antibody-mediated clustering of beta 1 integrins lacking the C-terminal 13 amino acids also induces clustering of alpha -actinin (24). However, alpha -actinin binding to clustered integrins is not sufficient to recruit F-actin (24, 32). Overexpression of alpha -actinin in fibroblasts leads to more stable attachment sites whereas isolated integrin-binding fragments of alpha -actinin disrupt stress fibers, FA, and shear-induced mechanical signaling in fibroblasts and osteoblasts (8, 31).


View larger version (20K):
[in this window]
[in a new window]
 
Fig. 2.   Models for integrin localization of actin nucleation and polymerization. VASP, profilin, Arp2/3, and WASP may regulate actin filament assembly at sites of integrin-ECM contact. Nck-2-WASP interactions have not been demonstrated but are hypothesized on the basis of Nck-1 binding to WASP.

Other Integrin-binding Cytoskeletal Proteins-- Recent reports suggest that additional proteins may serve as direct links between integrin tails and the cytoskeleton. In platelets, the two tyrosines in the beta 3 cytoplasmic tail become phosphorylated during agonist-induced cell aggregation (33). Synthetic peptides corresponding to the tyrosine-phosphorylated beta 3 tail bind to the actin-binding protein, myosin (34). This interaction may be physiologically relevant because conversion of the two beta 3 tail tyrosines to phenylalanine is associated with a mild bleeding phenotype in mice (33). Skelemin, a cytoskeletal M-band protein, can bind beta 1 and beta 3 but not beta 2 tails expressed in vitro (35). Skelemin co-localizes with stably expressed alpha IIbbeta 3 under some conditions, and microinjection of the integrin-binding domain of skelemin causes myoblasts to round up (35). Whether these interactions represent widespread or specialized cases of integrin-cytoskeleton linkages remains to be determined.

Vinculin-mediated Interactions-- Vinculin, an ~120-kDa molecule, is one of the most abundant FA proteins and interacts with F-actin, talin, alpha -actinin, paxillin, and vasodilator-stimulated phosphoprotein (VASP) (8, 36). Vinculin does not bind directly to integrins but may be recruited by integrin-bound talin or alpha -actinin (Fig. 1). However, although reduced levels of vinculin result in a reduction in the mechanical stiffness of the integrin-cytoskeleton linkage and increased cell motility, vinculin-null ES cells can differentiate in vitro into a variety of cell types (37) and can spread and form talin-rich FA and stress fibers (21). Thus, despite ubiquitous expression, vinculin is not absolutely required for some integrin-F-actin linkages and is likely to function as a molecular bridge to stabilize pre-existing linkages.

    Inside-out Integrin Signaling: Role of Cytoskeletal Proteins
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

Integrins are subject to rapid regulation of their ligand binding activity by intracellular signals, and this has been termed inside-out signaling or integrin activation (38). Inside-out signaling may act by 1) inducing conformational changes in and altering the affinity of integrin heterodimers and 2) clustering heterodimers into multimers. These forms of modulation are not mutually exclusive, and they may operate in a complementary manner to control both ligand binding and postligand binding events (39).

Inside-out signals to integrins originate from diverse plasma membrane receptors. As with signal propagation to other parts of the cell, these excitatory receptors presumably regulate integrins by triggering post-translational changes, such as phosphorylation/dephosphorylation, that affect the activity and/or subcellular localization of key enzymes and substrates in integrin-regulatory pathways (40). Thus, cytoskeletal proteins could modulate inside-out signaling by promoting the activity of integrin-regulatory molecules and/or by controlling their proximity to integrin cytoplasmic tails (38). Alternatively, or in addition, certain cytoskeletal proteins might be able to modulate the integrin activation state directly as the result of regulated changes in integrin-cytoskeleton linkages. Furthermore, in cases where integrins bind to counter-receptors on other cells instead of ECM, integrin avidity may be influenced by cytoskeleton-driven alignment of the membranes on the opposing cells (41).

As a possible example of regulation of integrin function by cytoskeletal linkages, beta 2 integrins from unstimulated neutrophils do not engage beta 2 ligands, and they co-immunoprecipitate with talin but not alpha -actinin (16). However, cell activation by fMet-Leu-Phe induces ligand binding to the beta 2 integrins and stimulates talin proteolysis and dissociation from beta 2 in a manner dependent on the calcium-dependent protease, calpain. During a later phase of cell activation, beta 2 now co-precipitates with alpha -actinin and not talin, an association hypothesized to result from a change in conformation of the beta 2 cytoplasmic tail (16). In this scheme, integrin activation would be initiated by calpain-dependent release of one integrin-cytoskeleton linkage and later reinforced by another. This overall model may also apply to activation of other integrins, but the precise details may differ. For example, calpain activation in platelets is a relatively late event, occurring after the initial phase of alpha IIbbeta 3 activation, and it is responsible for cleavage of numerous cytoskeletal and signaling proteins, including the beta 3 cytoplasmic tail itself (42).

Regulated interactions between cytoskeletal proteins and integrin cytoplasmic tails might also explain why alpha Lbeta 2 in phorbol ester-stimulated Epstein-Barr virus-transformed B lymphocytes exhibits a 10-fold increase in random diffusion rate, a change that correlates with increased cell adhesion to ICAM-1 (41). Treatment of these cells with low concentrations of cytochalasin D, which caps actin filaments preventing further polymerization, has the same effect, whereas higher concentrations of cytochalasin D inhibit cell adhesion. Similarly, exposure of peripheral blood lymphocytes to cytochalasins induces clustering of alpha Lbeta 2 and adhesion of the cells to ICAM-1 (43), and the same is observed in peripheral blood-derived T lymphoblasts after cross-linking of the T cell receptor (44). In leukocytes, it has been proposed that L-plastin, an actin-bundling protein, may modulate the avidity of alpha Mbeta 2 in a manner dependent on L-plastin phosphorylation by protein kinase C (45).

Cytoskeletal linkages may also be involved in the activation of alpha IIbbeta 3 in platelets. For example, in unstimulated platelets a subpopulation of alpha IIbbeta 3 is associated with the membrane cytoskeleton, and relatively low concentrations of cytochalasin D or latrunculin A, which blocks polymerization of actin monomers, induce ligand binding to alpha IIbbeta 3 (46). This effect requires a stimulus, such as ADP released from the washed platelets, which the authors suggest might increase actin turnover by binding to purinergic receptors and stimulating the actin filament-severing activity of gelsolin and the filament-disassembly activity of ADF-cofilin.

Rho family GTPases play a prominent role in actin polymerization and reorganization during cell migration (9), and it is logical to consider whether they are directly involved in promoting integrin activation. In fibroblasts, activation of Cdc42 and Rac is associated with the formation of focal complexes (9), but their effects on ligand binding to integrins has not been studied. Inhibition of Rho with C3 exoenzyme decreases beta 2 and beta 3 integrin-dependent aggregation of leukocytes and platelets, respectively (2). However, in adherent platelets inhibition of Rho with C3 exoenzyme blocks certain postligand binding events, such as the formation of vinculin patches and actin cables, but it has no effect on agonist-induced activation and ligand binding to alpha IIbbeta 3 (47). Similarly, C3 exoenzyme blocks the formation of FA and stress fibers in fibroblasts, but it has no significant effect on the activation state of alpha 5beta 1 (48). In these cases, therefore, Rho may function to regulate cell adhesion through effects on postligand binding events (9).

    Integrin-associated Proteins Regulate Actin Filament Assembly
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

The studies pointing to a role for actin and actin-binding proteins in regulating integrin function have coincided with remarkable recent advances in understanding the regulation of actin filament assembly. Integrins may provide the appropriate subcellular locale for actin filament assembly and organization in adherent and migratory cells by virtue of integrin-cytoskeleton linkages and integrin-triggered outside-in signals. In this context, several proteins implicated in the regulation of actin assembly are either components of FA or interact with cytoskeletal proteins that are linked to integrin beta  cytoplasmic tails.

The Mena/VASP Family-- Members of this protein family, which include VASP, the Drosophila protein Enabled (Ena), its mammalian orthologue Mena, and Evl (Ena-VASP-like), contain conserved N- and C-terminal domains (EVH1 and EVH2) separated by a proline-rich domain that binds profilin and SH3 domains (49, 50) (Fig. 2). The VASP EVH2 domain mediates tetramerization of the molecule, F-actin binding, and bundle formation (51). The EVH1 domain mediates targeting to FA by binding to proline-rich motifs in zyxin and vinculin (Fig. 2) and binds to the ActA movement protein of the intracellular bacteria Listeria monocytogenes (49, 50). Mena/VASP proteins are localized to sites of actin assembly, such as FA and membrane ruffles, and are concentrated at the tips of rapidly moving lamellipodia and at the focal contacts at their base (52). This localization of VASP is consistent with its proposed role in linking membrane proteins, which presumably include integrins, to polymerizing actin.

VASP is also a substrate for cyclic AMP-dependent protein kinase A and cyclic GMP-dependent protein kinase G. In platelets, cyclic AMP and cyclic GMP are potent inhibitors of agonist-induced activation of alpha IIbbeta 3, and phosphorylation of VASP by protein kinase A or protein kinase G correlates with inhibition of fibrinogen binding to activated platelets (53). There may be a causal relationship between VASP phosphorylation and inhibition of alpha IIbbeta 3 activation because VASP-deficient murine platelets show enhanced agonist-induced fibrinogen binding to alpha IIbbeta 3 and the inhibitory effects of cyclic nucleotides on fibrinogen binding are reduced (49, 53).

Investigation of ActA has provided insight into eukaryotic mechanisms for regulating actin filament assembly (54). This has led to a model in which Mena/VASP proteins are targeted to FA by binding to zyxin or vinculin, which in turn bind alpha -actinin or talin. This would allow Mena/VASP to bind to actin filaments via their EVH2 domains or through profilin that is bound to oligomerized Mena/VASP (Fig. 2). Microinjection of peptides that inhibit EVH-1 binding to vinculin and zyxin displace Mena/VASP from FA and cause retraction of membrane protrusions. Furthermore, a recessive lethal Ena allele contains a point mutation that impairs zyxin binding in vitro. Consequently, Mena/VASP function probably requires its targeting to FA via interactions with alpha -actinin (54). Surprisingly, mice deficient in VASP or Mena are viable, fertile, and display relatively mild phenotypes, which may reflect functional compensation by related family members (49, 50, 53). Mena-deficient mice that are also heterozygous for a profilin-1 deletion die perinatally. Thus, a 50% reduction in profilin-1 sensitizes animals to loss of Mena, consistent with their cooperation in regulating the actin cytoskeleton (50).

In summary, Mena/VASP proteins appear to contribute to F-actin binding at FA but are not required for FA assembly or maintenance. Mena/VASP proteins play important roles in regulating actin filament assembly, particularly at the leading edge of migrating cells, and Mena/VASP associations with integrins, although indirect, may target actin polymerization to fresh sites of integrin-ECM contact.

Arp2/3 and WASP-- The studies on Listeria, which highlighted the role of Mena/VASP, also revealed a requirement for the Arp2/3 complex for actin polymerization (54, 55). This complex consists of seven proteins and co-localizes with Mena/VASP at the leading edges of cells to promote the assembly of actin filament networks (55). Hence, recruitment of Arp2/3 to focal contacts containing integrin-associated Mena/VASP may contribute to actin assembly at sites of ECM contact (54). Machesky and Insall (55) describe a model for the activation of Arp2/3 by extracellular signals, leading to regulated assembly of actin filaments allowing production of force for cell motility and shape changes. A critical question in this model is how the Arp2/3 complex becomes localized at sites where actin polymerization is required, such as lamellipodia.

Identification of members of the WASP (Wiskott-Aldrich syndrome protein) family as Arp2/3-binding proteins (55) suggests a complex multimolecular assembly, which may bring Arp2/3 into contact with integrin-associated Mena/VASP (Fig. 2). Expression of WASP appears to be limited to cells of hematopoietic lineage; however, two family members, N-WASP and WAVE, have more widespread distributions (56). WASP proteins are proline-rich scaffolding molecules and effectors of the small GTPases, Cdc42 and Rac1 (56). WASP family members bind to actin, either through a direct interaction or via profilin or Arp2/3, and so may mediate some of the effects of Cdc42 or Rac on the cytoskeleton (57). Overexpression of WASP or N-WASP in mammalian cells leads to co-localization of F-actin with the overexpressed protein, and WASP-coated beads accumulate F-actin and exhibit motility within cells (56).

A model for Shigella motility suggests that co-localization of vinculin, VASP, profilin, and N-WASP may drive actin polymerization (58). Although speculative, such co-localization may also occur in vivo via associations of Nck, PINCH, and ILK (integrin linked kinase) with integrins (Fig. 2). ILK was identified as a binding protein of the integrin beta 1 and beta 3 tails (59), and ankyrin repeats within ILK appear to mediate binding to the LIM domain-only protein PINCH and recruit it to integrin complexes in spreading cells (59). PINCH also interacts with Nck-2, an SH2/SH3-containing protein, and so mediates an association between Nck-2 and ILK (59). The C-terminal SH3 domain of the closely related adapter protein Nck-1 binds to WASP (56). This domain is 75% identical to the corresponding Nck-2 SH3 domain, suggesting that a protein complex containing integrin, ILK, PINCH, Nck-2, WASP, and Arp2/3 might localize actin polymerization to sites of integrin-ECM contact in the lamellipodia of migrating cells. Some support for this hypothesis comes from unc-97 mutants in Caenorhabditis elegans. The UNC-97 protein belongs to the PINCH family of LIM domain proteins and is co-localized with beta  integrin at dense bodies (60), where it is required for the assembly and stability of these FA-like structures (60).

In conclusion, integrins associate with the actin cytoskeleton through a number of molecular linkages. In most cells, binding of the beta  integrin cytoplasmic tail to talin is an early and important step and probably provides a preliminary connection, which is reinforced by subsequent binding of alpha -actinin and vinculin. In turn, these proteins probably function to bring additional F-actin to the adhesion site, and they may also recruit zyxin, Mena/VASP, and profilin. Recruitment of WASP and Arp2/3 may lead to further actin polymerization and reorganization. The large number of actin-binding proteins within matrix adhesions and their numerous structural and functional interactions with integrins provide an important basis for the control of cellular functions by integrins.

    FOOTNOTES

* This minireview will be reprinted in the 2000 Minireview Compendium, which will be available in December, 2000. This is the second article of four in the "Integrins Minireview Series." The authors acknowledge the support of the National Institutes of Health.

To whom correspondence should be addressed. Tel.: 858-784-7124; Fax: 858-784-7343; E-mail: ginsberg@scripps.edu.

Published, JBC Papers in Press, May 4, 2000, DOI 10.1074/jbc.R900037199

    ABBREVIATIONS

The abbreviations used are: ECM, extracellular matrix; FA, focal adhesions; ERM, ezrin, radixin, and moesin; VASP, vasodilator-stimulated phosphoprotein; WASP, Wiskott-Aldrich syndrome protein; ILK, integrin-linked kinase.

    REFERENCES
TOP
INTRODUCTION
Role of Integrin Cytoplasmic...
Specific Integrin-Cytoskeleton...
Inside-out Integrin Signaling:...
Integrin-associated Proteins...
REFERENCES

1. Choquet, D., Felsenfeld, D. P., and Sheetz, M. P. (1997) Cell 88, 39-48
2. Burridge, K., and Chrzanowska-Wodnicka, M. (1996) Annu. Rev. Cell Dev. Biol. 12, 463-518
3. Liu, S., Thomas, S. M., Woodside, D. G., Rose, D. M., Kiosses, W. B., Pfaff, M., and Ginsberg, M. H. (1999) Nature 402, 676-681
4. Muir, T. W., Williams, M. J., Ginsberg, M. H., and Kent, S. B. H. (1994) Biochemistry 33, 7701-7708
5. Haas, T. A., and Plow, E. F. (1996) J. Biol. Chem. 271, 6017-6026
6. Leisner, T. M., Wencel-Drake, J. D., Wang, W., and Lam, S. C. (1999) J. Biol. Chem. 274, 12945-12949
7. Zamir, E., Katz, B. Z., Aota, S., Yamada, K. M., Geiger, B., and Kam, Z. (1999) J. Cell Sci. 112, 1655-1669
8. Jockusch, B. M., Bubeck, P., Giehl, K., Kroemker, M., Moschner, J., Rothkegel, M., Rudiger, M., Schluter, K., Stanke, G., and Winkler, J. (1995) Annu. Rev. Cell Dev. Biol. 11, 379-416
9. Hall, A. (1998) Science 23, 509-514
10. Reszka, A. A., Hayashi, Y., and Horwitz, A. F. (1992) J. Cell Biol. 117, 1321-1330
11. Ylanne, J., Huuskonen, J., O'Toole, T. E., Ginsberg, M. H., Virtanen, I., and Gahmberg, C. G. (1995) J. Biol. Chem. 270, 9550-9557
12. Peter, K., and O'Toole, T. E. (1995) J. Exp. Med. 181, 315-326
13. Schultz, J., Milpetz, F., Bork, P., and Ponting, C. P. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 5857-5864
14. Borowsky, M. L., and Hynes, R. O. (1998) J. Cell Biol. 143, 429-442
15. Pfaff, M., Liu, S., Erle, D. J., and Ginsberg, M. H. (1998) J. Biol. Chem. 273, 6104-6109
16. Sampath, R., Gallagher, P. J., and Pavalko, F. M. (1998) J. Biol. Chem. 273, 33588-33594
17. Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., and Ginsberg, M. H. (1999) J. Biol. Chem. 274, 28071-28074
18. Patil, S., Jedsadayanmata, A., Wencel-Drake, J. J., Wang, W., Knezevic, I., and Lam, S. C. T. (1999) J. Biol. Chem. 274, 28575-28583
19. Moulder, G. L., Huang, M. M., Waterston, R. H., and Barstead, R. J. (1996) Mol. Biol. Cell 7, 1181-1193
20. Albiges-Rizo, C., Frachet, P., and Block, M. R. (1995) J. Cell Sci. 108, 3317-3329
21. Priddle, H., Hemmings, L., Monkley, S., Woods, A., Patel, B., Sutton, D., Dunn, G. A., Zicha, D., and Critchley, D. R. (1998) J. Cell Biol. 142, 1121-1133
22. Kaapa, A., Peter, K., and Ylanne, J. (1999) Exp. Cell Res. 250, 524-534
23. Tapley, P., Horwitz, A., Buck, C. A., Duggan, K., and Rohrschneider, L. (1989) Oncogene 4, 325-333
24. Lewis, J. M., and Schwartz, M. A. (1995) Mol. Biol. Cell 6, 151-160
25. Ohta, Y., Suzuki, N., Nakamura, S., Hartwig, J. H., and Stossel, T. P. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 2122-2128
26. Fox, J. W., Lamperti, E. D., Eksioglu, Y. Z., Hong, S. E., Feng, Y., Graham, D. A., Scheffer, I. E., Dobyns, W. B., Hirsch, B. A., Radtke, R. A., Berkovic, S. F., Huttenlocher, P. R., and Walsh, C. A. (1998) Neuron 21, 1315-1325
27. Sharma, C. P., Ezzell, R. M., and Arnaout, M. A. (1995) J. Immunol. 154, 3461-3470
28. Glogauer, M., Arora, P., Chou, D., Janmey, P. A., Downey, G. P., and McCulloch, C. A. (1998) J. Biol. Chem. 273, 1689-1698
29. Cunningham, C. C., Gorlin, J. B., Kwiatkowski, D. J., Hartwig, J. H., Janmey, P. A., Byers, H. R., and Stossel, T. P. (1992) Science 255, 325-327
30. Meyer, S. C., Sanan, D. A., and Fox, J. E. (1998) J. Biol. Chem. 273, 3013-3020
31. Pavalko, F. M., Chen, N. X., Turner, C. H., Burr, D. B., Atkinson, S., Hsieh, Y. F., Qiu, J., and Duncan, R. L. (1998) Am. J. Physiol. 275, C1591-C1601
32. Cattelino, A., Albertinazzi, C., Bossi, M., Critchley, D. R., and de Curtis, I. (1999) Mol. Biol. Cell 10, 373-391
33. Law, D. A., DeGuzman, F. R., Heiser, P., Ministri-Madrid, K., Killeen, N., and Phillips, D. R. (1999) Nature 401, 808-811
34. Jenkins, A. L., Nannizzi-Alaimo, L., Silver, D., Sellers, J. R., Ginsberg, M. H., Law, D. A., and Phillips, D. R. (1998) J. Biol. Chem. 273, 13878-13885
35. Reddy, K. B., Gascard, P., Price, M. G., Negrescu, E. V., and Fox, J. E. B. (1998) J. Biol. Chem. 273, 35039-35047
36. Bubeck, P., Pistor, S., Wehland, J., and Jockusch, B. M. (1997) J. Cell Sci. 110, 1361-1371
37. Xu, W., Baribault, H., and Adamson, E. D. (1998) Development 125, 327-337
38. Hughes, P., and Pfaff, M. (1998) Trends Cell Biol. 8, 359-364
39. Hato, T., Pampori, N., and Shattil, S. J. (1998) J. Cell Biol. 141, 1685-1695
40. Pawson, T., and Scott, J. D. (1997) Science 278, 2075-2080
41. Kucik, D. F., Dustin, M. L., Miller, J. M., and Brown, E. J. (1996) J. Clin. Invest. 97, 2139-2144
42. Du, X., Saido, T. C., Tsubuki, S., Indig, F. E., Williams, M. J., and Ginsberg, M. H. (1995) J. Biol. Chem. 270, 26146-26151
43. Lub, M., van Kooyk, Y., van Vliet, S. J., and Figdor, C. G. (1997) Mol. Biol. Cell 8, 341-351
44. Stewart, M. P., McDowall, A., and Hogg, N. (1998) J. Cell Biol. 140, 699-707
45. Jones, S. L., Wang, J., Turck, C. W., and Brown, E. J. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 9331-9336
46. Bennett, J. S., Zigmond, S., Vilaire, G., Cunningham, M. E., and Bednar, B. (1999) J. Biol. Chem. 274, 25301-25307
47. Leng, L., Kashiwagi, H., Ren, X. D., and Shattil, S. J. (1998) Blood 91, 4206-4215
48. Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A. M., and Burridge, K. (1998) J. Cell Biol. 141, 539-551
49. Aszodi, A., Pfeifer, A., Ahmad, M., Glauner, M., Zhou, X. H., Ny, L., Andersson, K. E., Kehrel, B., Offermanns, S., and Fassler, R. (1999) EMBO J. 18, 37-48
50. Lanier, L. M., Gates, M. A., Witke, W., Menzies, A. S., Wehman, A. M., Macklis, J. D., Kwiatkowski, D., Soriano, P., and Gertler, F. B. (1999) Neuron 22, 313-325
51. Bachmann, C., Fischer, L., Walter, U., and Reinhard, M. (1999) J. Biol. Chem. 274, 23549-23557
52. Rottner, K., Behrendt, B., Small, J. V., and Weland, J. (1999) Nat. Cell Biol. 1, 321-322
53. Hauser, W., Knobeloch, K. P., Eigenthaler, M., Gambaryan, S., Krenn, V., Geiger, J., Glazova, M., Rohde, E., Horak, I., Walter, U., and Zimmer, M. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 8120-8125
54. Beckerle, M. C. (1998) Cell 95, 741-748
55. Machesky, L. M., and Insall, R. H. (1999) J. Cell Biol. 146, 267-272
56. Snapper, S. B., and Rosen, F. S. (1999) Annu. Rev. Immunol. 17, 905-929
57. Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T., and Kirschner, M. W. (1999) Cell 97, 221-231
58. Suzuki, T., Miki, H., Takenawa, T., and Sasakawa, C. (1998) EMBO J. 17, 2767-2776
59. Dedhar, S., Williams, B., and Hannigan, G. (1999) Trends Cell Biol. 9, 319-323
60. Hobert, O., Moerman, D. G., Clark, K. A., Beckerle, M. C., and Ruvkun, G. (1999) J. Cell Biol. 144, 45-57


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Immunol.Home page
J. M. Huston, M. Rosas-Ballina, X. Xue, O. Dowling, K. Ochani, M. Ochani, M. M. Yeboah, P. K. Chatterjee, K. J. Tracey, and C. N. Metz
Cholinergic Neural Signals to the Spleen Down-Regulate Leukocyte Trafficking via CD11b
J. Immunol., July 1, 2009; 183(1): 552 - 559.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
A. Asai, F. Okajima, K. Nakagawa, D. Ibusuki, K. Tanimura, Y. Nakajima, M. Nagao, M. Sudo, T. Harada, T. Miyazawa, et al.
Phosphatidylcholine hydroperoxide-induced THP-1 cell adhesion to intracellular adhesion molecule-1
J. Lipid Res., May 1, 2009; 50(5): 957 - 965.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
L. Cui, C. Chen, T. Xu, J. Zhang, X. Shang, J. Luo, L. Chen, X. Ba, and X. Zeng
c-Abl Kinase Is Required for {beta}2 Integrin-Mediated Neutrophil Adhesion
J. Immunol., March 1, 2009; 182(5): 3233 - 3242.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
D. S. Harburger and D. A. Calderwood
Integrin signalling at a glance
J. Cell Sci., January 15, 2009; 122(2): 159 - 163.
[Full Text] [PDF]


Home page
J. Cell Sci.Home page
M. Vicente-Manzanares, C. K. Choi, and A. R. Horwitz
Integrins in cell migration - the actin connection
J. Cell Sci., January 15, 2009; 122(2): 199 - 206.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
M. L. Heuze, I. Lamsoul, M. Baldassarre, Y. Lad, S. Leveque, Z. Razinia, C. Moog-Lutz, D. A. Calderwood, and P. G. Lutz
ASB2 targets filamins A and B to proteasomal degradation
Blood, December 15, 2008; 112(13): 5130 - 5140.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
P. Mertins, H. C. Eberl, J. Renkawitz, J. V. Olsen, M. L. Tremblay, M. Mann, A. Ullrich, and H. Daub
Investigation of Protein-tyrosine Phosphatase 1B Function by Quantitative Proteomics
Mol. Cell. Proteomics, September 1, 2008; 7(9): 1763 - 1777.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
H. Hirata, H. Tatsumi, and M. Sokabe
Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
J. Cell Sci., September 1, 2008; 121(17): 2795 - 2804.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
J. M. Auger and S. P. Watson
Dynamic Tyrosine Kinase-Regulated Signaling and Actin Polymerisation Mediate Aggregate Stability Under Shear
Arterioscler. Thromb. Vasc. Biol., August 1, 2008; 28(8): 1499 - 1504.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. R. Thom, V. M. Bhopale, D. J. Mancini, and T. N. Milovanova
Actin S-Nitrosylation Inhibits Neutrophil {beta}2 Integrin Function
J. Biol. Chem., April 18, 2008; 283(16): 10822 - 10834.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
N. Yu, L. Erb, R. Shivaji, G. A. Weisman, and C. I. Seye
Binding of the P2Y2 Nucleotide Receptor to Filamin A Regulates Migration of Vascular Smooth Muscle Cells
Circ. Res., March 14, 2008; 102(5): 581 - 588.
[Abstract] [Full Text] [PDF]


Home page
Proc Am Thorac SocHome page
W. Zhang and S. J. Gunst
Interactions of Airway Smooth Muscle Cells with Their Tissue Matrix: Implications for Contraction
Proceedings of the ATS, January 1, 2008; 5(1): 32 - 39.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. Zhang, Y. Wu, C. Wu, and S. J. Gunst
Integrin-linked Kinase Regulates N-WASp-mediated Actin Polymerization and Tension Development in Tracheal Smooth Muscle
J. Biol. Chem., November 23, 2007; 282(47): 34568 - 34580.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Vielreicher, G. Harms, E. Butt, U. Walter, and A. Obergfell
Dynamic Interaction between Src and C-terminal Src Kinase in Integrin {alpha}IIbbeta3-mediated Signaling to the Cytoskeleton
J. Biol. Chem., November 16, 2007; 282(46): 33623 - 33631.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
J. Zhu, C. V. Carman, M. Kim, M. Shimaoka, T. A. Springer, and B.-H. Luo
Requirement of {alpha} and {beta} subunit transmembrane helix separation for integrin outside-in signaling
Blood, October 1, 2007; 110(7): 2475 - 2483.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
X. Shi, Y.-Q. Ma, Y. Tu, K. Chen, S. Wu, K. Fukuda, J. Qin, E. F. Plow, and C. Wu
The MIG-2/Integrin Interaction Strengthens Cell-Matrix Adhesion and Modulates Cell Motility
J. Biol. Chem., July 13, 2007; 282(28): 20455 - 20466.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
G. Bix, R. A. Iozzo, B. Woodall, M. Burrows, A. McQuillan, S. Campbell, G. B. Fields, and R. V. Iozzo
Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the {alpha}2{beta}1-integrin receptor
Blood, May 1, 2007; 109(9): 3745 - 3748.
[Abstract] [Full Text] [PDF]


Home page
IOVSHome page
A. J. LaGier, S. H. Yoo, E. C. Alfonso, S. Meiners, and M. E. Fini
Inhibition of Human Corneal Epithelial Production of Fibrotic Mediator TGF-{beta}2 by Basement Membrane-Like Extracellular Matrix
Invest. Ophthalmol. Vis. Sci., March 1, 2007; 48(3): 1061 - 1071.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
G. R. Van de Walle, A. Schoolmeester, B. F. Iserbyt, J. M. E. M. Cosemans, J. W. M. Heemskerk, M. F. Hoylaerts, A. Nurden, K. Vanhoorelbeke, and H. Deckmyn
Activation of {alpha}IIb{beta}3 is a sufficient but also an imperative prerequisite for activation of {alpha}2{beta}1 on platelets
Blood, January 15, 2007; 109(2): 595 - 602.
[Abstract] [Full Text] [PDF]


Home page
Journals of Gerontology Series A: Biological Sciences and Medical SciencesHome page
X. Chen, Z. Li, Z. Feng, J. Wang, C. Ouyang, W. Liu, B. Fu, G. Cai, C. Wu, R. Wei, et al.
Integrin-Linked Kinase Induces Both Senescence-Associated Alterations and Extracellular Fibronectin Assembly in Aging Cardiac Fibroblasts
J. Gerontol. A Biol. Sci. Med. Sci., December 1, 2006; 61(12): 1232 - 1245.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
H. Pan, J. Xie, F. Ye, and S.-J. Gao
Modulation of Kaposi's Sarcoma-Associated Herpesvirus Infection and Replication by MEK/ERK, JNK, and p38 Multiple Mitogen-Activated Protein Kinase Pathways during Primary Infection.
J. Virol., June 1, 2006; 80(11): 5371 - 5382.
[Abstract] [Full Text] [PDF]


Home page
IOVSHome page
M. S. Filla, A. Woods, P. L. Kaufman, and D. M. Peters
{beta}1 and {beta}3 Integrins Cooperate to Induce Syndecan-4-Containing Cross-linked Actin Networks in Human Trabecular Meshwork Cells
Invest. Ophthalmol. Vis. Sci., May 1, 2006; 47(5): 1956 - 1967.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
M. V. Hernandez, M. G. D. Sala, J. Balsamo, J. Lilien, and C. O. Arregui
ER-bound PTP1B is targeted to newly forming cell-matrix adhesions
J. Cell Sci., April 1, 2006; 119(7): 1233 - 1243.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
A. Wiedemann, J. C. Patel, J. Lim, A. Tsun, Y. van Kooyk, and E. Caron
Two distinct cytoplasmic regions of the {beta}2 integrin chain regulate RhoA function during phagocytosis.
J. Cell Biol., March 27, 2006; 172(7): 1069 - 1079.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
M. R. Tardif and M. J. Tremblay
Regulation of LFA-1 Activity through Cytoskeleton Remodeling and Signaling Components Modulates the Efficiency of HIV Type-1 Entry in Activated CD4+ T Lymphocytes
J. Immunol., July 15, 2005; 175(2): 926 - 935.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
M. A. Rosenthal-Allieri, M. Ticchioni, J. P. Breittmayer, Y. Shimizu, and A. Bernard
Influence of {beta}1 Integrin Intracytoplasmic Domains in the Regulation of VLA-4-Mediated Adhesion of Human T Cells to VCAM-1 under Flow Conditions
J. Immunol., July 15, 2005; 175(2): 1214 - 1223.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
S. Incerpi
Thyroid Hormones: Rapid Reply by Surface Delivery Only
Endocrinology, July 1, 2005; 146(7): 2861 - 2863.
[Full Text] [PDF]


Home page
J. Cell Sci.Home page
D. J. Powner, R. M. Payne, T. R. Pettitt, M. L. Giudici, R. F. Irvine, and M. J. O. Wakelam
Phospholipase D2 stimulates integrin-mediated adhesion via phosphatidylinositol 4-phosphate 5-kinase I{gamma}b
J. Cell Sci., July 1, 2005; 118(13): 2975 - 2986.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
S. L. Hooper and J. B. Thuma
Invertebrate Muscles: Muscle Specific Genes and Proteins
Physiol Rev, July 1, 2005; 85(3): 1001 - 1060.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
J. J. Bergh, H.-Y. Lin, L. Lansing, S. N. Mohamed, F. B. Davis, S. Mousa, and P. J. Davis
Integrin {alpha}V{beta}3 Contains a Cell Surface Receptor Site for Thyroid Hormone that Is Linked to Activation of Mitogen-Activated Protein Kinase and Induction of Angiogenesis
Endocrinology, July 1, 2005; 146(7): 2864 - 2871.
[Abstract] [Full Text] [PDF]


Home page
Br. J. Radiol.Home page
V Meineke
The role of damage to the cutaneous system in radiation-induced multi-organ failure
Br. J. Radiol., January 1, 2005; Supplement_27(1): 95 - 99.
[Abstract] [Full Text] [PDF]


Home page
DevelopmentHome page
R. S. Schmid, S. Shelton, A. Stanco, Y. Yokota, J. A. Kreidberg, and E. S. Anton
{alpha}3{beta}1 integrin modulates neuronal migration and placement during early stages of cerebral cortical development
Development, December 15, 2004; 131(24): 6023 - 6031.
[Abstract] [Full Text] [PDF]


Home page
Endocr. Rev.Home page
D. D. Mruk and C. Y. Cheng
Sertoli-Sertoli and Sertoli-Germ Cell Interactions and Their Significance in Germ Cell Movement in the Seminiferous Epithelium during Spermatogenesis
Endocr. Rev., October 1, 2004; 25(5): 747 - 806.
[Abstract] [Full Text] [PDF]


Home page
Journals of Gerontology Series A: Biological Sciences and Medical SciencesHome page
Z. Li, X. Chen, Y. Xie, S. Shi, Z. Feng, B. Fu, X. Zhang, G. Cai, C. Wu, D. Wu, et al.
Expression and Significance of Integrin-Linked Kinase in Cultured Cells, Normal Tissue, and Diseased Tissue of Aging Rat Kidneys
J. Gerontol. A Biol. Sci. Med. Sci., October 1, 2004; 59(10): B984 - B996.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Zhang, K. Chen, Y. Tu, and C. Wu
Distinct Roles of Two Structurally Closely Related Focal Adhesion Proteins, {alpha}-Parvins and {beta}-Parvins, in Regulation of Cell Morphology and Survival
J. Biol. Chem., October 1, 2004; 279(40): 41695 - 41705.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
S. J. Shattil and P. J. Newman
Integrins: dynamic scaffolds for adhesion and signaling in platelets
Blood, September 15, 2004; 104(6): 1606 - 1615.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
A. Bronstad, A. Berg, and R. K. Reed
Effects of the taxanes paclitaxel and docetaxel on edema formation and interstitial fluid pressure
Am J Physiol Heart Circ Physiol, August 1, 2004; 287(2): H963 - H968.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
J. M. Gibbins
Platelet adhesion signalling and the regulation of thrombus formation
J. Cell Sci., July 15, 2004; 117(16): 3415 - 3425.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. A. Calderwood, V. Tai, G. Di Paolo, P. De Camilli, and M. H. Ginsberg
Competition for Talin Results in Trans-dominant Inhibition of Integrin Activation
J. Biol. Chem., July 9, 2004; 279(28): 28889 - 28895.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
J.-i. Kawabe, S. Okumura, M.-C. Lee, J. Sadoshima, and Y. Ishikawa
Translocation of caveolin regulates stretch-induced ERK activity in vascular smooth muscle cells
Am J Physiol Heart Circ Physiol, May 1, 2004; 286(5): H1845 - H1852.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
N. Sharma-Walia, P. P. Naranatt, H. H. Krishnan, L. Zeng, and B. Chandran
Kaposi's Sarcoma-Associated Herpesvirus/Human Herpesvirus 8 Envelope Glycoprotein gB Induces the Integrin-Dependent Focal Adhesion Kinase-Src-Phosphatidylinositol 3-Kinase-Rho GTPase Signal Pathways and Cytoskeletal Rearrangements
J. Virol., April 15, 2004; 78(8): 4207 - 4223.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
D. A. Calderwood
Integrin activation
J. Cell Sci., March 1, 2004; 117(5): 657 - 666.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
P. Prahalad, I. Calvo, H. Waechter, J. B. Matthews, A. Zuk, and K. S. Matlin
Regulation of MDCK cell-substratum adhesion by RhoA and myosin light chain kinase after ATP depletion
Am J Physiol Cell Physiol, March 1, 2004; 286(3): C693 - C707.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
S.-M. Kim, M. S. Kwon, C. S. Park, K.-R. Choi, J.-S. Chun, J. Ahn, and W. K. Song
Modulation of Thr Phosphorylation of Integrin {beta}1 during Muscle Differentiation
J. Biol. Chem., February 20, 2004; 279(8): 7082 - 7090.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
C. V. Carman, C.-D. Jun, A. Salas, and T. A. Springer
Endothelial Cells Proactively Form Microvilli-Like Membrane Projections upon Intercellular Adhesion Molecule 1 Engagement of Leukocyte LFA-1
J. Immunol., December 1, 2003; 171(11): 6135 - 6144.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
S. Attwell, J. Mills, A. Troussard, C. Wu, and S. Dedhar
Integration of Cell Attachment, Cytoskeletal Localization, and Signaling by Integrin-linked Kinase (ILK), CH-ILKBP, and the Tumor Suppressor PTEN
Mol. Biol. Cell, December 1, 2003; 14(12): 4813 - 4825.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. S. Orange, K. E. Harris, M. M. Andzelm, M. M. Valter, R. S. Geha, and J. L. Strominger
The mature activating natural killer cell immunologic synapse is formed in distinct stages
PNAS, November 25, 2003; 100(24): 14151 - 14156.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. Fukuda and G. W. Schmid-Schonbein
Regulation of CD18 expression on neutrophils in response to fluid shear stress
PNAS, November 11, 2003; 100(23): 13152 - 13157.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
S. Tadokoro, S. J. Shattil, K. Eto, V. Tai, R. C. Liddington, J. M. de Pereda, M. H. Ginsberg, and D. A. Calderwood
Talin Binding to Integrin {beta} Tails: A Final Common Step in Integrin Activation
Science, October 3, 2003; 302(5642): 103 - 106.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
F. Baluska, J. Samaj, P. Wojtaszek, D. Volkmann, and D. Menzel
Cytoskeleton-Plasma Membrane-Cell Wall Continuum in Plants. Emerging Links Revisited
Plant Physiology, October 1, 2003; 133(2): 482 - 491.
[Full Text] [PDF]


Home page
BloodHome page
S. Feng, J. C. Resendiz, X. Lu, and M. H. Kroll
Filamin A binding to the cytoplasmic tail of glycoprotein Ib{alpha} regulates von Willebrand factor-induced platelet activation
Blood, September 15, 2003; 102(6): 2122 - 2129.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
I. L. Barsukov, A. Prescot, N. Bate, B. Patel, D. N. Floyd, N. Bhanji, C. R. Bagshaw, K. Letinic, G. Di Paolo, P. De Camilli, et al.
Phosphatidylinositol Phosphate Kinase Type 1{gamma} and {beta}1-Integrin Cytoplasmic Domain Bind to the Same Region in the Talin FERM Domain
J. Biol. Chem., August 15, 2003; 278(33): 31202 - 31209.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B.-Z. Katz, L. Romer, S. Miyamoto, T. Volberg, K. Matsumoto, E. Cukierman, B. Geiger, and K. M. Yamada
Targeting Membrane-localized Focal Adhesion Kinase to Focal Adhesions: ROLES OF TYROSINE PHOSPHORYLATION AND SRC FAMILY KINASES
J. Biol. Chem., August 1, 2003; 278(31): 29115 - 29120.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. M. Akula, P. P. Naranatt, N.-S. Walia, F.-Z. Wang, B. Fegley, and B. Chandran
Kaposi's Sarcoma-Associated Herpesvirus (Human Herpesvirus 8) Infection of Human Fibroblast Cells Occurs through Endocytosis
J. Virol., July 15, 2003; 77(14): 7978 - 7990.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
S. J. Gunst and J. J. Fredberg
The first three minutes: smooth muscle contraction, cytoskeletal events, and soft glasses
J Appl Physiol, July 1, 2003; 95(1): 413 - 425.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
U. Tigges, B. Koch, J. Wissing, B. M. Jockusch, and W. H. Ziegler
The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase C{alpha}
J. Biol. Chem., June 20, 2003; 278(26): 23561 - 23569.
[Abstract] [Full Text] [PDF]


Home page
DevelopmentHome page
K. A. Clark, M. McGrail, and M. C. Beckerle
Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
Development, June 15, 2003; 130(12): 2611 - 2621.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
B. Hinz, V. Dugina, C. Ballestrem, B. Wehrle-Haller, and C. Chaponnier
{alpha}-Smooth Muscle Actin Is Crucial for Focal Adhesion Maturation in Myofibroblasts
Mol. Biol. Cell, June 1, 2003; 14(6): 2508 - 2519.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Buensuceso, M. de Virgilio, and S. J. Shattil
Detection of Integrin alpha IIbbeta 3 Clustering in Living Cells
J. Biol. Chem., April 18, 2003; 278(17): 15217 - 15224.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
C. J. Loy, K. S. Sim, and E. L. Yong
Filamin-A fragment localizes to the nucleus to regulate androgen receptor and coactivator functions
PNAS, April 15, 2003; 100(8): 4562 - 4567.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
W. Baumgartner, G. J. Schutz, J. Wiegand, N. Golenhofen, and D. Drenckhahn
Cadherin function probed by laser tweezer and single molecule fluorescence in vascular endothelial cells
J. Cell Sci., March 15, 2003; 116(6): 1001 - 1011.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
Y. Zhang, K. Chen, Y. Tu, A. Velyvis, Y. Yang, J. Qin, and C. Wu
Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
J. Cell Sci., March 14, 2003; 115(24): 4777 - 4786.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Oda, I. Wada, K. Miura, K. Okawa, T. Kadoya, T. Kato, H. Nishihara, M. Maeda, S. Tanaka, K. Nagashima, et al.
CrkL Directs ASAP1 to Peripheral Focal Adhesions
J. Biol. Chem., February 14, 2003; 278(8): 6456 - 6460.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. Butler, M. P. Williams, and S. D. Blystone
Ligand-dependent Activation of Integrin alpha vbeta 3
J. Biol. Chem., February 7, 2003; 278(7): 5264 - 5270.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M.-P. Manitz, B. Horst, S. Seeliger, A. Strey, B. V. Skryabin, M. Gunzer, W. Frings, F. Schonlau, J. Roth, C. Sorg, et al.
Loss of S100A9 (MRP14) Results in Reduced Interleukin-8-Induced CD11b Surface Expression, a Polarized Microfilament System, and Diminished Responsiveness to Chemoattractants In Vitro
Mol. Cell. Biol., February 1, 2003; 23(3): 1034 - 1043.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
R. R. Hantgan, D. S. Lyles, T. C. Mallett, M. Rocco, C. Nagaswami, and J. W. Weisel
Ligand Binding Promotes the Entropy-driven Oligomerization of Integrin alpha IIbbeta 3
J. Biol. Chem., January 24, 2003; 278(5): 3417 - 3426.
[Abstract] [Full Text] [PDF]


Home page
J AndrolHome page
W.-Y. Lui, D. D. Mruk, W. M. Lee, and C. Y. Cheng
Adherens Junction Dynamics in the Testis and Spermatogenesis
J Androl, January 1, 2003; 24(1): 1 - 14.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Zhang, K. Chen, L. Guo, and C. Wu
Characterization of PINCH-2, a New Focal Adhesion Protein That Regulates the PINCH-1-ILK Interaction, Cell Spreading, and Migration
J. Biol. Chem., October 4, 2002; 277(41): 38328 - 38338.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Jin and J. Li
Dynamitin Controls beta 2 Integrin Avidity by Modulating Cytoskeletal Constraint on Integrin Molecules
J. Biol. Chem., August 30, 2002; 277(36): 32963 - 32969.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
M. M. Monick, L. Powers, N. Butler, T. Yarovinsky, and G. W. Hunninghake
Interaction of matrix with integrin receptors is required for optimal LPS-induced MAP kinase activation
Am J Physiol Lung Cell Mol Physiol, August 1, 2002; 283(2): L390 - L402.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Bertoni, S. Tadokoro, K. Eto, N. Pampori, L. V. Parise, G. C. White, and S. J. Shattil
Relationships between Rap1b, Affinity Modulation of Integrin alpha IIbbeta 3, and the Actin Cytoskeleton
J. Biol. Chem., July 5, 2002; 277(28): 25715 - 25721.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Arai, J. A. Spencer, and E. N. Olson
STARS, a Striated Muscle Activator of Rho Signaling and Serum Response Factor-dependent Transcription
J. Biol. Chem., June 28, 2002; 277(27): 24453 - 24459.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
H.-N. Fournier, S. Dupe-Manet, D. Bouvard, M.-L. Lacombe, C. Marie, M. R. Block, and C. Albiges-Rizo
Integrin Cytoplasmic Domain-associated Protein 1alpha (ICAP-1alpha ) Interacts Directly with the Metastasis Suppressor nm23-H2, and Both Proteins Are Targeted to Newly Formed Cell Adhesion Sites upon Integrin Engagement
J. Biol. Chem., May 31, 2002; 277(23): 20895 - 20902.
[Abstract] [Full Text] [PDF]


Home page
J. Leukoc. Biol.Home page
J. D. Borgquist, M. T. Quinn, and S. D. Swain
Adhesion to extracellular matrix proteins modulates bovine neutrophil responses to inflammatory mediators
J. Leukoc. Biol., May 1, 2002; 71(5): 764 - 774.
[Abstract] [Full Text] [PDF]


Home page
Biol. Reprod.Home page
T. A. Towle, P. C.W. Tsang, R. A. Milvae, M. K. Newbury, and J. A. McCracken
Dynamic In Vivo Changes in Tissue Inhibitors of Metalloproteinases 1 and 2, and Matrix Metalloproteinases 2 and 9, During Prostaglandin F2{alpha}-Induced Luteolysis in Sheep
Biol Reprod, May 1, 2002; 66(5): 1515 - 1521.
[Abstract] [Full Text]


Home page
J. Cell Sci.Home page
T. Ohashi, D. P. Kiehart, and H. P. Erickson
Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants
J. Cell Sci., March 15, 2002; 115(6): 1221 - 1229.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
S.-Y. Shai, A. E. Harpf, C. J. Babbitt, M. C. Jordan, M. C. Fishbein, J. Chen, M. Omura, T. A. Leil, K. D. Becker, M. Jiang, et al.
Cardiac Myocyte-Specific Excision of the {beta}1 Integrin Gene Results in Myocardial Fibrosis and Cardiac Failure
Circ. Res., March 8, 2002; 90(4): 458 - 464.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Bot.Home page
M. J. Jaffe, A. C. Leopold, and R. C. Staples
Thigmo responses in plants and fungi
Am. J. Botany, March 1, 2002; 89(3): 375 - 382.
[Abstract] [Full Text] [PDF]


Home page
Cell Growth Differ.Home page
T. L. Davis, F. Buerger, and A. E. Cress
Differential Regulation of a Novel Variant of the {alpha}6 Integrin, {alpha}6p
Cell Growth Differ., March 1, 2002; 13(3): 107 - 113.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Datta, F. Huber, and D. Boettiger
Phosphorylation of beta 3 Integrin Controls Ligand Binding Strength
J. Biol. Chem., February 1, 2002; 277(6): 3943 - 3949.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
J. C. Adams
Regulation of protrusive and contractile cell-matrix contacts
J. Cell Sci., January 15, 2002; 115(2): 257 - 265.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
S. J. Hyduk and M. I. Cybulsky
{alpha}4 Integrin Signaling Activates Phosphatidylinositol 3-Kinase and Stimulates T Cell Adhesion to Intercellular Adhesion Molecule-1 to a Similar Extent As CD3, but Induces a Distinct Rearrangement of the Actin Cytoskeleton
J. Immunol., January 15, 2002; 168(2): 696 - 704.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
A. E. Aplin, B. P. Hogan, J. Tomeu, and R. L. Juliano
Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases
J. Cell Sci., January 7, 2002; 115(13): 2781 - 2790.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
C. Schreider, G. Peignon, S. Thenet, J. Chambaz, and M. Pincon-Raymond
Integrin-mediated functional polarization of Caco-2 cells through E-cadherin--actin complexes
J. Cell Sci., January 2, 2002; 115(3): 543 - 552.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
Y. Liu, B. P.-C. Chen, M. Lu, Y. Zhu, M. B. Stemerman, S. Chien, and J. Y.-J. Shyy
Shear Stress Activation of SREBP1 in Endothelial Cells Is Mediated by Integrins
Arterioscler. Thromb. Vasc. Biol., January 1, 2002; 22(1): 76 - 81.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Wang, E. S. Boja, W. Tan, E. Tekle, H. M. Fales, S. English, J. J. Mieyal, and P. B. Chock
Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells
J. Biol. Chem., December 14, 2001; 276(51): 47763 - 47766.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Biederer and T. C. Sudhof
CASK and Protein 4.1 Support F-actin Nucleation on Neurexins
J. Biol. Chem., December 14, 2001; 276(51): 47869 - 47876.
[Abstract] [Full Text] [PDF]


Home page
Clin. Cancer Res.Home page
N. D. Zantek, J. Walker-Daniels, J. Stewart, R. K. Hansen, D. Robinson, H. Miao, B. Wang, H.-J. Kung, M. J. Bissell, and M. S. Kinch
MCF-10A-NeoST: A New Cell System for Studying Cell-ECM and Cell-Cell Interactions in Breast Cancer
Clin. Cancer Res., November 1, 2001; 7(11): 3640 - 3648.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
C. Ruiz, C.-Y. Liu, Q.-H. Sun, M. Sigaud-Fiks, E. Fressinaud, J.-Y. Muller, P. Nurden, A. T. Nurden, P. J. Newman, and N. Valentin
A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa ({alpha}IIb{beta}3) integrin receptor locked in a high-affinity state and a Glanzmann thrombasthenia-like phenotype
Blood, October 15, 2001; 98(8): 2432 - 2441.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
P. Piccardoni, R. Sideri, S. Manarini, A. Piccoli, N. Martelli, G. de Gaetano, C. Cerletti, and V. Evangelista
Platelet/polymorphonuclear leukocyte adhesion: a new role for SRC kinases in Mac-1 adhesive function triggered by P-selectin
Blood, July 1, 2001; 98(1): 108 - 116.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
W. J. Bruyninckx, K. M. Comerford, D. W. Lawrence, and S. P. Colgan
Phosphoinositide 3-kinase modulation of {beta}3-integrin represents an endogenous "braking" mechanism during neutrophil transmatrix migration
Blood, May 15, 2001; 97(10): 3251 - 3258.
[Abstract] [Full Text] [PDF]


Home page
JEMHome page
J. R. Chan, S. J. Hyduk, and M. I. Cybulsky
Chemoattractants Induce a Rapid and Transient Upregulation of Monocyte {alpha}4 Integrin Affinity for Vascular Cell Adhesion Molecule 1 Which Mediates Arrest: An Early Step in the Process of Emigration
J. Exp. Med., May 14, 2001; 193(10): 1149 - 1158.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
Y. Tu, Y. Huang, Y. Zhang, Y. Hua, and C. Wu
A New Focal Adhesion Protein that Interacts with Integrin-linked Kinase and Regulates Cell Adhesion and Spreading
J. Cell Biol., April 30, 2001; 153(3): 585 - 598.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
A. E. Aplin, S. A. Stewart, R. K. Assoian, and R.L. Juliano
Integrin-mediated adhesion Regulates ERK Nuclear Translocation and Phosphorylation of Elk-1
J. Cell Biol., April 9, 2001; 153(2): 273 - 282.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Wang, H. Chen, and E. J. Brown
L-plastin Peptide Activation of alpha vbeta 3-mediated Adhesion Requires Integrin Conformational Change and Actin Filament Disassembly
J. Biol. Chem., April 20, 2001; 276(17): 14474 - 14481.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Obergfell, B. A. Judd, M. A. del Pozo, M. A. Schwartz, G. A. Koretzky, and S. J. Shattil
The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin alpha IIbbeta 3 to the Actin Cytoskeleton
J. Biol. Chem., February 16, 2001; 276(8): 5916 - 5923.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Li, N. Wong, M. D. Jabali, and P. Johnson
CD44-initiated Cell Spreading Induces Pyk2 Phosphorylation, Is Mediated by Src Family Kinases, and Is Negatively Regulated by CD45
J. Biol. Chem., July 27, 2001; 276(31): 28767 - 28773.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. D'Addario, P. D. Arora, J. Fan, B. Ganss, R. P. Ellen, and C. A. G. McCulloch
Cytoprotection against Mechanical Forces Delivered through beta 1 Integrins Requires Induction of Filamin A
J. Biol. Chem., August 17, 2001; 276(34): 31969 - 31977.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Boettiger, L. Lynch, S. Blystone, and F. Huber
Distinct Ligand-binding Modes for Integrin alpha vbeta 3-Mediated Adhesion to Fibronectin versus Vitronectin
J. Biol. Chem., August 17, 2001; 276(34): 31684 - 31690.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
X. Zhou, J. Li, and D. F. Kucik
The Microtubule Cytoskeleton Participates in Control of beta 2 Integrin Avidity
J. Biol. Chem., November 21, 2001; 276(48): 44762 - 44769.
[Abstract] [Full Text] [PDF]


This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
275/30/22607    most recent
R900037199v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Calderwood, D. A.
Right arrow Articles by Ginsberg, M. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Calderwood, D. A.
Right arrow Articles by Ginsberg, M. H.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement