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J Biol Chem, Vol. 274, Issue 46, 32531-32534, November 12, 1999
From the Structural Biology Laboratory, The Salk Institute for
Biological Studies, La Jolla, California 92037
Actin polymerization is required for many types
of cell motility, such as chemotaxis, nerve growth cone movement, cell
spreading, and platelet activation (reviewed in Ref. 1). In the
lamellipodia that push forward the leading edge of motile cells,
polymerizing filaments form a meshwork consisting of "Y branches"
with the pointed end of one filament attached to the side of another
filament (2). This meshwork presumably may provide a rigid body against which polymerization can drive membrane protrusion (3).
A major unanswered question is how cells integrate signals coming
through a variety of pathways to control when and where actin
polymerizes. The filaments grow from a huge pool of unpolymerized actin
maintained by monomer-binding proteins at a concentration approximately
1000-fold higher than required for spontaneous polymerization of actin
(reviewed in Ref. 4). The monomer-binding protein profilin biases the
direction of filament elongation, allowing growth at the fast growing
barbed end but not the slow growing pointed end (reviewed in Ref. 4).
In cells capping proteins block the barbed end of most filaments, so
some mechanism is required to start new filaments (5).
Cells might trigger actin polymerization in three ways: 1) de
novo nucleation of filaments from monomeric actin; 2) severing existing filaments to create uncapped barbed ends; and 3) uncapping existing barbed ends. There is evidence for each of these mechanisms in
various cellular processes, but new filaments are often created during
cell motility (6), placing emphasis on mechanisms 1 and 2.
Although activation of de novo nucleation by cell
stimulation has long been an attractive model (7), no barbed end
nucleating factors were known until it was discovered that Arp2/3
complex promotes actin nucleation, creating filaments that grow at
their barbed ends (8). Because nucleation is rate-limiting in actin polymerization and strongly suppressed by monomer-binding proteins, Arp2/3 complex may be a key mediator of actin polymerization in cells.
Arp2/3 complex also cross-links actin filaments end-to-side, indistinguishable from the Y branches at the leading edge (8).
Based on these biochemical activities, Mullins et al. (8)
proposed the dendritic nucleation model, whereby Arp2/3 complex both
creates new filaments and cross-links them into a branching meshwork.
Cellular observations support this model. Arp2/3 complex is
concentrated at the leading edge of motile cells (9-13), specifically at the junctions of the Y branches (12, 13). It exists in all
eukaryotes examined, and ablation of Arp2/3 complex subunits in
Saccharomyces cerevisiae and Schizosaccharomyces
pombe is lethal or severely debilitating (14-21).
The next breakthrough was the discovery that ActA, a cell surface
protein from the pathogenic bacterium, Listeria
monocytogenes, stimulates Arp2/3 complex to nucleate actin
in vitro (22). Listeria uses force generated by
actin polymerization to propel itself around the cytoplasm of
eukaryotic cells. ActA is the only bacterial protein required to induce
polymerization, but ActA cannot stimulate actin filament formation by
itself (reviewed in Ref. 23). This work suggested that cellular factors
might activate Arp2/3 complex to nucleate actin.
This year WASp/Scar proteins were identified as the first example of
such factors (24-28). These proteins also interact with a variety of
cell signaling molecules known to influence cytoskeletal dynamics,
bringing us closer to forging a connection between surface receptor
stimulation and actin polymerization. The rapid progress reviewed here
depended upon groundwork from many laboratories. Analysis of
Wiskott-Aldrich syndrome protein (WASp) and its neural homolog N-WASP
revealed a binding site for Rho family GTPases and other domains that
affect actin assembly in cells (29, 30). Study of
GTP The Arp2/3 complex contains one copy of each of seven strongly
associated protein subunits (Fig. 1;
reviewed in detail in Ref. 38). Arp2 and Arp3 are actin-related
proteins. The other five subunits are novel. The complex is very
abundant, approximately 2 µM in the cytoplasm of
Acanthamoeba (9). Analysis of molecular models of Arp2 and
Arp3 first led to the hypothesis that they form a stable dimer that
binds the pointed end of actin filaments and nucleates growth in the
barbed direction (9). Polymerization assays established that the
complex binds the pointed end with nanomolar affinity and has modest
nucleation activity (8).
The mammalian WASp/Scar family currently consists of five members:
WASp, N-WASP, and three Scar isoforms (Fig.
2). Several lines of evidence implicate
these proteins in actin polymerization. The gene encoding WASp,
apparently expressed only in hematopoietic cells, is mutated in
Wiskott-Aldrich syndrome, an X-linked human disease with selective
defects in platelet development and lymphocytes (29). The presence of a
binding motif (GBD) for activated Cdc42 and Rac hinted that WASp might
regulate actin, because these Rho family GTPases influence actin
dynamics and because transfection of WASp rearranges actin filaments in
cultured cells (39). The WASp homologue N-WASP is expressed more widely
in vertebrate cells than WASp (30) and causes filopodial formation when
co-expressed with Cdc42 in cultured cells (40). Scar was discovered in
Dictyostelium where disruption of its gene rescues the
developmental defect caused by disruption of a cyclic AMP receptor
(41). Deletion of Scar in wild type cells causes cytoskeletal defects.
A mammalian homologue of Scar, termed WAVE or Scar1, might be involved
in Rac-induced membrane ruffling, although it does not contain a GBD
(42). No information is yet available on the functions of two other
human Scar-related open reading frames (GenBank accession numbers
BAA74923 and CAA18609). In S. cerevisiae, a WASp/Scar homologue, known as Las17p or Bee1p, is essential for cortical actin
patch formation and for endocytosis (37, 43).
The C-terminal 65-105 amino acids of WASp/Scar proteins (Fig.
3) enhance nucleation by Arp2/3 complex
(25-28). This region starts with a WASp homology 2 (WH2) motif, a
16-19-amino acid sequence that participates in actin monomer binding
(24). N-WASP has two tandem WH2 motifs. The C-terminal 15-20 residues,
designated "A," generally possess a strongly negative net charge
and interact with Arp2/3 complex (24). Between these two regions are
30-40 residues of unknown functional significance. Some have suggested that this region of WASp and N-WASP contains a short sequence similar
to the actin monomer-binding protein cofilin ("cofilin homology
domain"), although in our opinion the sequence similarity is too
limited to indicate homology (Fig. 3). Furthermore, these short
sequences cannot be a domain in the usual sense, because in
ADF/cofilins they form part of a
MINIREVIEW
Regulation of Actin Polymerization by Arp2/3 Complex and
WASp/Scar Proteins*
INTRODUCTION
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INTRODUCTION
Properties of Arp2/3 Complex
The WASp/Scar Protein Family
Actin Filament Nucleation by...
Many Questions Still to...
Final Comments
REFERENCES
S1-stimulated actin
polymerization in extracts of vertebrate cells (31-34),
Dictyostelium (33), and Acanthamoeba (35)
demonstrated that the Rho family GTPase Cdc42 mediates the effect of
GTP and that Arp2/3 complex is required. Similar experiments with
extracted yeast suggested that Bee1p (a WASp homolog) and Arp2/3
complex are required for actin patch assembly (20, 36, 37).
Properties of Arp2/3 Complex
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INTRODUCTION
Properties of Arp2/3 Complex
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Actin Filament Nucleation by...
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Final Comments
REFERENCES
View larger version (25K):
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Fig. 1.
Arp 2/3 complex structure.
Left, two-dimensional model, based on nearest
neighbor relationships of the subunits from chemical cross-linking and
two-hybrid data. Circles are proportional to subunit masses,
also indicated by molecular masses in kDa. Right, very low
resolution structural model, based on nearest neighbors, hydrodynamic
properties, and electron microscopy.
The WASp/Scar Protein Family
TOP
INTRODUCTION
Properties of Arp2/3 Complex
The WASp/Scar Protein Family
Actin Filament Nucleation by...
Many Questions Still to...
Final Comments
REFERENCES
View larger version (22K):
[in a new window]
Fig. 2.
Domain/motif structures of WASp/Scar
proteins. Black, WH1; blue, GBD;
yellow, polyproline (numbers correspond to number
of stretches of five or more prolines); green, WH2;
red, acidic (numbers correspond to numbers of
acidic/basic residues).
-strand, a loop, and part of an
-helix rather than an independently folded structure (44). However,
there is evidence that this region participates in binding actin
monomers (45).
View larger version (18K):
[in a new window]
Fig. 3.
Sequence alignment of WASp/Scar activation
regions. All are human sequences except Bee1 and Verprolin
(budding yeast) and D. Scar (Dictyostelium).
Numbers in parentheses represent the starting
residue in the alignment. Acidic residues in A region are in
red. Highly conserved residues in WH2 motif are in
green. Basic residues in WH2 motif are in
blue.
The C terminus of Las17p/Bee1p differs significantly from other WASp/Scar proteins. In its WH2 motif, it has two unique inserts of unknown significance. The region between WH2 and A motifs differs even more, with >50% of this sequence consisting of G, A, or P. Perhaps more importantly, Bee1p is the only WASp/Scar protein in which the C-terminal 20 residues have a net neutral charge (excluding the C-terminal carboxyl group, Fig. 3). These differences might explain some functional differences of Bee1p (27).
N-terminal to this nucleation-activating region, WASp and N-WASP bind an impressive list of protein ligands (Table I): the Rho family GTPases Cdc42 and Rac, WASp-interacting protein, calmodulin, Src kinases, Tec kinases, Grb2, Nck, and profilin. These proteins provide a myriad of possibilities to regulate either the activity or location of WASp or N-WASP. No interacting proteins for Scar1 other than actin, profilin, and Arp2/3 complex have been identified.
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WASp and N-WASp also have an N-terminal WASp homology 1 domain (WH1).
An atomic structure of an EVH1 domain, a homolog of the WH1 domain
found in adapter proteins including Ena and VASP, shows that the fold
of the domain is similar to a pleckstrin homology domain (57). Ligands
with the sequence FPPPP bind EVH1 in the place of an intrinsic
-helix found in pleckstrin homology domains, which can bind
PIP2. PIP2 apparently binds an N-terminal
construct of N-WASP (30) and activates nucleation by full-length N-WASP (26), but more detailed work defining the binding site is needed.
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Actin Filament Nucleation by Arp2/3 Complex and WASp/Scar Proteins |
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Machesky and Insall (24) found that human WASp and Scar1 interact with the p21 subunit in two-hybrid assay and with the whole complex in biochemical assays. Introduction of pieces of these proteins into cultured cells disrupts membrane ruffling and delocalizes Arp2/3 complex. The minimum Scar fragment sufficient for these effects on cells contains the WH2 and acidic (WA) motifs. The same Scar fragment greatly enhances actin nucleation by Arp2/3 complex, reducing the lag time and increasing the number of filaments (25).
WASp/Scar proteins activate nucleation of actin filaments by Arp2/3
complex (Fig. 4). To understand the mechanism one must first appreciate
how actin behaves by itself. Nucleation by actin monomers alone is very
unfavorable because of the instability of actin dimers and trimers,
obligate intermediates on the pathway to filaments (reviewed in Ref.
4). Unfavorable nucleation accounts for the lag at the onset of
spontaneous polymerization. During the lag trimers form immediately,
but the bulk rate of polymerization is low because the concentration of
these nuclei is exceedingly low. Trimers have a lifetime of
microseconds because of rapid dissociation to dimers and the rare
addition of actin monomers to form a stable filament. The number of
filaments accumulates during the reaction, mainly by nucleation but
also by infrequent breaks into two filaments. Early in the reaction,
end to end annealing consumes a significant number of filament ends. At
any point in the reaction the concentration of filament barbed ends can
be calculated from the polymerization rate (polymerization rate = [ends]((k+) [actin monomers] 
(k
)).
Arp2/3 complex alone promotes polymerization, but the reaction is inefficient (8). The kinetic data are best fit by a model where the complex captures actin dimers, which then grow into filaments by addition of actin subunits at the barbed end. The model accounts for the inefficiency by the low concentration of dimers and by dissociation of 98% of captured dimers from the complex before producing a filament. The initial lag persists even with high concentrations of Arp2/3 complex.
Addition of C-terminal constructs of WASp/Scar proteins to Arp2/3
complex significantly decreases but does not eliminate the lag in
polymerization (Fig. 4A).
Together they also increase the number of filament ends, as reflected
by the large increase in slope of the polymerization curve.
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Addition of preformed actin filaments along with Arp2/3 complex and WASp/Scar constructs reduces the lag still further (Fig. 4A). This result suggests that the dendritic nucleation model is fundamentally correct; association of Arp2/3 complex with the side of an existing filament enhances its nucleation of a new filament. This hypothesis (Fig. 4B) explains the persistent lag in experiments with actin, Arp2/3, and WASp/Scar. More detailed work in our laboratory suggests that the lag with Arp2/3 complex and WASp is due to the buildup of filaments by spontaneous polymerization, with a threshold of <100 nM actin in filaments needed to activate Arp2/3 complex and WASp.2 The order of events is still unclear; Arp2/3 complex binds both the sides of actin filaments and WASp/Scar WA, so it could bind filaments either before or after association with WA and actin subunits.
The WH2 and A regions of Scar1 are required to stimulate nucleation by
Arp2/3 complex (25). The adjacent polyproline domain may favor one or
more steps in the reaction but is not absolutely required either in the
presence or absence of profilin. The A region of human Scar1 interacts
directly with the p21 subunit (24) but does not activate nucleation
(25). The A regions of N-WASP and WASp are also insufficient for Arp2/3
complex activation (26).3 On
the other hand, the A region (with an undefined N-terminal boundary) of
yeast Bee1p appears to activate nucleation by yeast Arp2/3 complex
(27). Although unlikely given the conservation of these molecules,
Bee1p may activate yeast Arp2/3 complex in a different way than other
WASp/Scar proteins. More detailed dissection of this region is needed
to determine the minimal functional WASp/Scar unit and the role of
actin monomer binding by WASp/Scar proteins in nucleation.
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Many Questions Still to Answer |
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Does All Leading Edge Actin Filament Nucleation Depend on Arp2/3 Complex?-- Two lines of evidence suggest that Arp2/3 complex plays a major role but do not rule out other pathways. First, most of the GTP-stimulated actin polymerization in cell extracts depends on Arp2/3 complex (32, 35), as does actin patch reconstitution in yeast (20). Second, most of the filaments at the leading edge of keratocytes and fibroblasts are incorporated into 70° branching networks with Arp2/3 complex localized at the branches (13). The affinities of Arp2/3 complex for both the pointed end and side of actin filaments allow the complex to form these branched networks (8, 58). WASp/Scar proteins are not required for branching by Arp2/3 complex but may stabilize either or both associations. On the other hand, experiments with budding yeast suggest alternative pathways. Neither Arp2 nor Arp3 is essential for viability, although null strains are extremely sick and the phenotype may depend on the genetic background of the particular strain (21).
What Signaling Pathways Converge on Arp2/3 Complex via WASp/Scar Proteins?-- A variety of stimuli regulates cellular actin polymerization, acting through receptor tyrosine kinase/mitogen-activated protein kinase pathways, seven helix receptors, and integrins. Details remain unclear, but an attractive hypothesis (24) is that signals from different kinds of receptors and signaling pathways converge on particular members of WASp/Scar proteins, which funnel these signals through Arp2/3 complex as a final common pathway to actin filament formation. Any of these signals could, in principle, affect either the activity of Arp2/3 complex or its localization in cells.
The only demonstrated activators for any WASp/Scar protein are Cdc42 and PIP2. Both activate N-WASP and Arp2/3 complex to nucleate actin filaments in vitro (26). Participation of Cdc42 and PIP2 in activating WASp/Scar does not restrict the upstream pathways, because seven-helix receptors, tyrosine kinase receptors, and integrins can all influence these signaling molecules (59, 60).
WASp-interacting protein, Grb2, Src kinases, Tec kinases, calmodulin, and Nck are other potential regulators of WASp/Scar proteins (Table I). Like Cdc42 and PIP2, multiple receptor classes might regulate most if not all of these proteins. These proteins could act in the same way as Cdc42 and PIP2, enabling WASp and N-WASP to activate Arp2/3 complex, but they might have other roles such as targeting WASp and N-WASP to particular parts of a cell. Any effect of WASp phosphorylation by Src or Tec kinases is entirely unclear. The identity of Scar activators is unknown, although the link between Scar and cAMP receptor in Dictyostelium suggests a role for seven-helix receptors and trimeric G-proteins.
Do Other Cellular Proteins Activate Arp2/3 Complex?-- Given the large number of potential regulatory proteins for WASp/Scar proteins, they alone may regulate actin filament nucleation mediated by Arp2/3 complex. However, the existence of ActA establishes a precedent for other protein activators. Posttranslational modifications of Arp2/3 complex subunits also need to be considered along with differential expression of two p41 ARC isoforms in mammals (10, 61).
Where Does Nucleation Take Place?-- It is not clear how WASp/Scar proteins and Arp2/3 complex interact with activators at the leading edge. Because the signal-activating nucleation often comes from a surface receptor and because many of the signal-transducing molecules that bind and/or activate WASp/Scar proteins are bound to receptors or membranes, they may activate Arp2/3 complex on the membrane (26). However, Arp2/3 complex is concentrated in the cortical actin filament network rather than on membranes (9, 10, 12, 13, 61, 62). Additional work is required to pinpoint the sites of Arp2/3 complex activation.
What Is the Role of Actin Monomer Binding by WASp/Scar Proteins?-- The C terminus of WASp/Scar binds monomeric actin (24, 30, 42), which might stabilize the nascent filament during nucleation (Fig. 4B). However, the way in which WASp/Scar C termini bind actin is not clear. In our hands, human WASp WA binds monomeric actin with a Kd of about 0.5 µM. It inhibits elongation at the pointed end but does not inhibit barbed end growth or sequester actin monomers.2 Scar1 behaves similarly (24). Others find that N-WASP WA and Scar1 WA depolymerize actin filaments (30, 40, 42, 45). One hypothesis proposed for N-WASP WA is that it severs actin filaments, thereby exposing new barbed ends for rapid elongation (40). However, the data for severing could be interpreted in other ways, such as actin monomer sequestration. In our hands, neither WASp WA nor Scar1 WA severs filaments or sequesters monomers.2
Does Profilin Participate in Actin Nucleation by Arp2/3 Complex and
WASp/Scar Proteins?--
Profilin is thought to participate in actin
dynamics as a nucleotide exchange factor (63) and carrier for subunits
during elongation (64), but the role of its interaction with
proline-rich sequences of WASp/Scar proteins in nucleation by Arp2/3
complex is unclear. WASp/Scar family members contain at least four
potential profilin-binding sites of 5 or more prolines (Fig. 2), and
some evidence suggests that profilin enhances the cellular activities of N-WASP and Scar1 (42, 56). In vitro profilin reduces
background nucleation, increasing the signal to noise of the Arp2/3
complex/Scar trigger for new filament formation (25). Scar1 PWA (with
potential profilin-binding sites) is more effective than Scar1 WA in
the presence of profilin, but the rate is lower than without profilin. Thus profilin interaction with the P domain does not enhance the activation of Arp2/3 complex. One idea is that profilin bound to
polyproline-containing ligands targets actin to nucleation or
elongation sites (65). We question this theory, because participation of profilin could only slow down diffusion-limited actin filament elongation rate and profilin inhibits nucleation.
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Final Comments |
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INTRODUCTION
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Final Comments
REFERENCES
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The recent results summarized here show that WASp/Scar proteins
stimulate the formation of new actin filaments by Arp2/3 complex. These
fascinating WASp/Scar proteins may in turn be regulated by several
signaling pathways. The enthusiasm for these new insights should not
lessen the attention given to other complementary mechanisms of actin
filament generation such as severing or uncapping. Work also needs to
continue on the mechanisms by which actin networks are disassembled to
recycle subunits to sites of growth.
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FOOTNOTES |
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* This minireview will be reprinted in the 1999 Minireview Compendium, which will be available in December, 1999. This is the first article of four in the "Proteins That Regulate Dynamic Actin Remodeling in Response to Membrane Signaling Minireview Series."
To whom correspondence should be addressed: The Salk Institute for
Biological Studies, 10010 North Torrey Pines Rd., La Jolla, CA 92037. Tel.: 619-453-4100 (ext. 1261); Fax: 619-452-0838; E-mail: pollard@salk.edu.
2 H. N. Higgs, L. Blanchoin, and T. D. Pollard, submitted for publication.
3 H. N. Higgs and T. D. Pollard, unpublished observations.
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ABBREVIATIONS |
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The abbreviations used are:
GTPS, guanosine
5'-3-O-(thio)triphosphate;
WH2, WASp homology 2;
WH1, WASp
homology 1;
PIP2, phosphatidylinositol 4,5-bisphosphate;
WA, WH2 and acidic;
A, acidic;
PWA, polyproline, WH2, and acidic;
GBD, GTPase-binding domain.
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INTRODUCTION
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Final Comments
REFERENCES
|
|---|
| 1. | Mitchison, T. J., and Cramer, L. P. (1996) Cell 84, 371-379[CrossRef][Medline] [Order article via Infotrieve] |
| 2. |
Svitkina, T. M.,
Verkhovsky, A. B.,
McQuade, K. M.,
and Borisy, G. G.
(1997)
J. Cell Biol.
139,
397-415 |
| 3. | Mogilner, A., and Oster, G. (1996) Biophys. J. 71, 3030-3045[Medline] [Order article via Infotrieve] |
| 4. | Pollard, T. D., and Cooper, J. A. (1986) Annu. Rev. Biochem. 55, 987-1035[CrossRef][Medline] [Order article via Infotrieve] |
| 5. |
Schafer, D. A.,
Jennings, P. B.,
and Cooper, J. A.
(1996)
J. Cell Biol.
135,
169-179 |
| 6. | Chan, A. Y., Raft, S., Bailly, M., Wyckoff, J. B., Segall, J. E., and Condeelis, J. S. (1998) J. Cell Sci. 111, 199-211[Abstract] |
| 7. |
Carson, M.,
Weber, A.,
and Zigmond, S. H.
(1986)
J. Cell Biol.
103,
2707-2714 |
| 8. |
Mullins, R. D.,
Heuser, J. A.,
and Pollard, T. D.
(1998)
Proc. Natl. Acad. Sci. U. S. A.
95,
6181-6186 |
| 9. |
Kelleher, J. F.,
Atkinson, S. J.,
and Pollard, T. D.
(1995)
J. Cell Biol.
131,
385-397 |
| 10. | Machesky, L. M., Reeves, E., Wientjes, F., Mattheyse, F. J., Grogan, A., Totty, N. F., Burlingame, A. L., Hsuan, J. J., and Segal, A. W. (1997) Biochem. J. 328, 105-112 |
| 11. |
Schafer, D. A.,
Welch, M. D.,
Machesky, L. M.,
Bridgman, P. C.,
Meyer, S. M.,
and Cooper, J. A.
(1998)
J. Cell Biol.
143,
1919-1930 |
| 12. |
Bailly, M.,
Macaluso, F.,
Cammer, M.,
Chan, A.,
Segall, J. E.,
and Condeelis, J. S.
(1999)
J. Cell Biol.
145,
331-345 |
| 13. |
Svitkina, T. M.,
and Borisy, G. G.
(1999)
J. Cell Biol.
145,
1009-1026 |
| 14. | Schwob, E., and Martin, R. P. (1992) Nature 355, 179-182[CrossRef][Medline] [Order article via Infotrieve] |
| 15. |
Lees-Miller, J. P.,
Henry, G.,
and Helfman, D. M.
(1992)
Proc. Natl. Acad. Sci. U. S. A.
89,
80-83 |
| 16. | Balasubramanian, M. K., Feoktistova, A., McCollum, D., and Gould, K. L. (1996) EMBO J. 15, 6426-6437[Medline] [Order article via Infotrieve] |
| 17. | McCollum, D., Feoktistova, A., Morphew, M., Balasubramanian, M., and Gould, K. L. (1996) EMBO J. 15, 6438-6446[Medline] [Order article via Infotrieve] |
| 18. |
Moreau, V.,
Madania, A.,
Martin, R. P.,
and Winsor, B.
(1996)
J. Cell Biol.
134,
117-132 |
| 19. | Moreau, V., Galan, J. M., Devilliers, G., Haguenauer-Tsapis, R., and Winsor, B. (1997) Mol. Biol. Cell 8, 1361-1375[Abstract] |
| 20. | Winter, D., Podtelejnikov, A. V., Mann, M., and Li, R. (1997) Curr. Biol. 7, 519-529[CrossRef][Medline] [Order article via Infotrieve] |
| 21. |
Winter, D. C.,
Choe, E. Y.,
and Li, R.
(1999)
Proc. Natl. Acad. Sci. U. S. A.
96,
7288-7293 |
| 22. |
Welch, M. D.,
Rosenblatt, J.,
Skoble, J.,
Portnoy, D. A.,
and Mitchison, T. J.
(1998)
Science
281,
105-108 |
| 23. | Cossart, P., and Lecuit, M. (1998) EMBO J. 17, 3797-3806[CrossRef][Medline] [Order article via Infotrieve] |
| 24. | Machesky, L. M., and Insall, R. H. (1998) Curr. Biol. 8, 1347-1356[CrossRef][Medline] [Order article via Infotrieve] |
| 25. |
Machesky, L. M.,
Mullins, D. M.,
Higgs, H. N.,
Kaiser, D. A.,
Blanchoin, L.,
May, R. C.,
Hall, M. E.,
and Pollard, T. D.
(1999)
Proc. Natl. Acad. Sci. U. S. A.
96,
3739-3744 |
| 26. | Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T., and Kirschner, M. W. (1999) Cell 97, 221-231[CrossRef][Medline] [Order article via Infotrieve] |
| 27. | Winter, D., Lechler, T., and Li, R. (1999) Curr. Biol. 9, 501-504[CrossRef][Medline] [Order article via Infotrieve] |
| 28. | Yarar, D., To, W., Abo, A., and Welch, M. D. (1999) Curr. Biol. 9, 555-558[CrossRef][Medline] [Order article via Infotrieve] |
| 29. | Ochs, H. D. (1998) Semin. Hematol. 35, 332-345[Medline] [Order article via Infotrieve] |
| 30. | Miki, H., Miura, K., and Takenawa, T. (1996) EMBO J. 15, 5326-5335[Medline] [Order article via Infotrieve] |
| 31. |
Ma, L.,
Cantley, L. C.,
Janmey, P. A.,
and Kirschner, M. W.
(1998)
J. Cell Biol.
140,
1125-1136 |
| 32. |
Ma, L.,
Rohatgi, R.,
and Kirschner, M. W.
(1998)
Proc. Natl. Acad. Sci. U. S. A.
95,
15362-15367 |
| 33. |
Zigmond, S. H.,
Joyce, M.,
Borleis, J.,
Bokoch, G. M.,
and Devreotes, P. N.
(1997)
J. Cell Biol.
138,
363-374 |
| 34. |
Zigmond, S. H.,
Joyce, M.,
Yang, C.,
Brown, K.,
Huang, M.,
and Pring, M.
(1998)
J. Cell Biol.
142,
1001-1012 |
| 35. | Mullins, R. D., and Pollard, T. D. (1999) Curr. Biol. 9, 405-415[CrossRef][Medline] [Order article via Infotrieve] |
| 36. |
Lechler, T.,
and Li, R.
(1997)
J. Cell Biol.
138,
95-103 |
| 37. |
Li, R.
(1997)
J. Cell Biol.
136,
649-658 |
| 38. | Mullins, R. D., and Pollard, T. D. (1999) Curr. Opin. Struct. Biol. 9, 244-249[CrossRef][Medline] [Order article via Infotrieve] |
| 39. | Symons, M., Derry, J. M. J., Kariak, B., Jiang, S., Lemahieu, V., McCormick, F., Francke, U., and Abo, A. (1996) Cell 84, 723-734[CrossRef][Medline] [Order article via Infotrieve] |
| 40. | Miki, H., Sasaki, T., Takai, Y., and Takenawa, T. (1998) Nature 391, 93-96[CrossRef][Medline] [Order article via Infotrieve] |
| 41. |
Bear, J. E.,
Rawls, J. F.,
and Saxe, C. L.
(1998)
J. Cell Biol.
142,
1325-1335 |
| 42. | Miki, H., Suetsugu, S., and Takenawa, T. (1998) EMBO J. 17, 6932-6941[CrossRef][Medline] [Order article via Infotrieve] |
| 43. | Naqvi, S. N., Zahn, R., Mitchell, D. A., Stevenson, B. J., and Munn, A. L. (1998) Curr. Biol. 8, 959-962[CrossRef][Medline] [Order article via Infotrieve] |
| 44. | Leonard, S. A., Gittis, A. G., Petrella, E. C., Pollard, T. D., and Lattman, E. E. (1997) Nat. Struct. Biol. 4, 369-373[CrossRef][Medline] [Order article via Infotrieve] |
| 45. | Miki, H., and Takenawa, T. (1998) Biochem. Biophys. Res. Commun. 243, 73-78[CrossRef][Medline] [Order article via Infotrieve] |
| 46. |
Rudolph, M. G.,
Bayer, P.,
Abo, A.,
Kuhlman, J.,
Vetter, I. R.,
and Wittinghofer, A.
(1998)
J. Biol. Chem.
273,
18067-18076 |
| 47. |
Ramesh, N.,
Anton, I. M.,
Hartwig, J. H.,
and Geha, R. S.
(1997)
Proc. Natl. Acad. Sci. U. S. A.
94,
14671-14676 |
| 48. |
Stewart, D. M.,
Tian, L.,
and Nelson, D. L.
(1999)
J. Immunol.
162,
5019-5024 |
| 49. | Banin, S., Truong, O., Katz, D. R., Waterfield, M. D., Brickell, P. M., and Cout, I. (1996) Curr. Biol. 6, 981-989[CrossRef][Medline] [Order article via Infotrieve] |
| 50. | Guinamard, R., Aspenstrom, P., Fougereau, M., Chavrier, P., and Guillemot, J. C. (1998) FEBS Lett. 434, 431-436[CrossRef][Medline] [Order article via Infotrieve] |
| 51. | Cory, G. O. C., MacCarthy-Morrogh, L., Banin, S., Gout, I., Brickell, P. M., Levinsky, R. J., Kinnon, C., and Lovering, R. C. (1996) J. Immunol. 157, 3791-3795[Abstract] |
| 52. |
Baba, Y.,
Nonoyama, S.,
Matsushita, M.,
Yamadori, T.,
Hashimoto, S.,
Imai, K.,
Arai, S.,
Kunikata, T.,
Kurimoto, M.,
Kurosaki, T.,
Ochs, H.,
Yata, J.,
Kishimoto, T.,
and Tsukada, S.
(1999)
Blood
93,
2003-2012 |
| 53. | She, H., Rockow, S., Tang, J., Nishimura, R., Skolnik, E. Y., Chen, M., Margolis, B., and Li, W. (1997) Mol. Biol. Cell 8, 1709-1721[Abstract] |
| 54. |
Oda, A.,
Ochs, H.,
Druker, D. J.,
Ozaki, K.,
Watanabe, C.,
Handa, M.,
Miyakawa, Y.,
and Ikeda, Y.
(1998)
Blood
92,
1852-1858 |
| 55. | Rivero-Lezcano, O. M., Marcilla, A., Sameshima, J. H., and Robbins, K. C. (1995) Mol. Cell. Biol. 15, 5725-5731[Abstract] |
| 56. | Suetsugu, S., Miki, H., and Takenawa, T. (1998) EMBO J. 17, 6516-6526[CrossRef][Medline] [Order article via Infotrieve] |
| 57. | Prehoda, K. E., Lee, D. J., and Lim, W. A. (1999) Cell, in press |
| 58. |
Mullins, R. D.,
Kelleher, J. F.,
Xu, J.,
and Pollard, T. D.
(1998)
Mol. Biol. Cell
9,
841-852 |
| 59. |
Hall, A.
(1998)
Science
279,
509-514 |
| 60. |
Pike, L. J.,
and Casey, L.
(1996)
J. Biol. Chem.
271,
26453-26456 |
| 61. |
Welch, M. D.,
DePace, A. H.,
Verma, S.,
Iwamatsu, A.,
and Mitchison, T. J.
(1997)
J. Cell Biol.
138,
375-384 |
| 62. |
Mullins, R. D.,
Stafford, W. F.,
and Pollard, T. D.
(1997)
J. Cell Biol.
136,
331-343 |
| 63. |
Blanchoin, L.,
and Pollard, T. D.
(1998)
J. Biol. Chem.
273,
25106-25111 |
| 64. | Pantaloni, D., and Carlier, M. F. (1993) Cell 75, 1007-1014[CrossRef][Medline] [Order article via Infotrieve] |
| 65. | Beckerle, M. C. (1998) Cell 95, 741-748[CrossRef][Medline] [Order article via Infotrieve] |
| 66. |
Vaduva, G.,
Martin, N. C.,
and Hopper, A. K.
(1997)
J. Cell Biol.
139,
1821-1833 |
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|
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|
|
|
|
|
|
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|
|
|
|
 |
|
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|
|
|
|
|
|
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|
|
|
|
|
|
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|
|
|
|
|
|
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|
|
|
|
|
|
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|
|
|
|
 |
|
 D. Pantaloni, C. L. Clainche, and M.-F. Carlier Mechanism of Actin-Based Motility Science, May 25, 2001; 292(5521): 1502 - 1506. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
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|
|
|
|
 |
|
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|
|
|
|
 |
|
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|
|
|
|
|
|
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|
|
|
|
|
|
B. Mayer SH3 domains: complexity in moderation J. Cell Sci., January 4, 2001; 114(7): 1253 - 1263. [Abstract] [PDF]
|
|
|
|
|
|
D Diviani and J. Scott AKAP signaling complexes at the cytoskeleton J. Cell Sci., January 4, 2001; 114(8): 1431 - 1437. [Abstract] [PDF]
|
|
|
|
|
|
E. Haddad, J. L. Zugaza, F. Louache, N. Debili, C. Crouin, K. Schwarz, A. Fischer, W. Vainchenker, and J. Bertoglio The interaction between Cdc42 and WASP is required for SDF-1-induced T-lymphocyte chemotaxis Blood, January 1, 2001; 97(1): 33 - 38. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
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|
|
|
|
|
|
H. Yamaguchi, H. Miki, S. Suetsugu, L. Ma, M. W. Kirschner, and T. Takenawa Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP PNAS, October 26, 2000; (2000) 190351397. [Abstract] [Full Text]
|
|
|
|
|
|
S. A. Weed, A. V. Karginov, D. A. Schafer, A. M. Weaver, A. W. Kinley, J. A. Cooper, and J. T. Parsons Cortactin Localization to Sites of Actin Assembly in Lamellipodia Requires Interactions with F-Actin and the Arp2/3 Complex J. Cell Biol., September 25, 2000; 151(1): 29 - 40. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. N. Higgs and T. D. Pollard Activation by Cdc42 and PIP2 of Wiskott-Aldrich Syndrome protein (WASp) Stimulates Actin Nucleation by Arp2/3 Complex J. Cell Biol., September 18, 2000; 150(6): 1311 - 1320. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. H. Zigmond How WASP Regulates Actin Polymerization J. Cell Biol., September 18, 2000; 150(6): F117 - F120. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Glogauer, J. Hartwig, and T. Stossel Two Pathways Through Cdc42 Couple the N-formyl Receptor to Actin Nucleation in Permeabilized Human Neutrophils J. Cell Biol., August 21, 2000; 150(4): 785 - 796. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M.-F. Carlier, F. Ressad, and D. Pantaloni Control of Actin Dynamics in Cell Motility. ROLE OF ADF/COFILIN J. Biol. Chem., November 26, 1999; 274(48): 33827 - 33830. [Full Text] [PDF]
|
|
|
|
|
|
H. Q. Sun, M. Yamamoto, M. Mejillano, and H. L. Yin Gelsolin, a Multifunctional Actin Regulatory Protein J. Biol. Chem., November 19, 1999; 274(47): 33179 - 33182. [Full Text] [PDF]
|
|
|
|
|
|
N. Volkmann, K. J. Amann, S. Stoilova-McPhie, C. Egile, D. C. Winter, L. Hazelwood, J. E. Heuser, R. Li, T. D. Pollard, and D. Hanein Structure of Arp2/3 Complex in Its Activated State and in Actin Filament Branch Junctions Science, September 28, 2001; 293(5539): 2456 - 2459. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Belisle and A. Abo N-Formyl Peptide Receptor Ligation Induces Rac-dependent Actin Reorganization through Gbeta gamma Subunits and Class Ia Phosphoinositide 3-Kinases J. Biol. Chem., August 18, 2000; 275(34): 26225 - 26232. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Silvin, B. Belisle, and A. Abo A Role for Wiskott-Aldrich Syndrome Protein in T-cell Receptor-mediated Transcriptional Activation Independent of Actin Polymerization J. Biol. Chem., June 8, 2001; 276(24): 21450 - 21457. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. I. Miller, M.-K. Chang, C. D. Funk, J. R. Feramisco, and J. L. Witztum 12/15-Lipoxygenase Translocation Enhances Site-specific Actin Polymerization in Macrophages Phagocytosing Apoptotic Cells J. Biol. Chem., May 25, 2001; 276(22): 19431 - 19439. [Abstract] [Full Text] [PDF]
|
|
|
|
|
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K. Hufner, H. N. Higgs, T. D. Pollard, C. Jacobi, M. Aepfelbacher, and S. Linder The Verprolin-like Central (VC) Region of Wiskott-Aldrich Syndrome Protein Induces Arp2/3 Complex-dependent Actin Nucleation J. Biol. Chem., September 14, 2001; 276(38): 35761 - 35767. [Abstract] [Full Text] [PDF]
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H. Yamaguchi, H. Miki, S. Suetsugu, L. Ma, M. W. Kirschner, and T. Takenawa Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP PNAS, November 7, 2000; 97(23): 12631 - 12636. [Abstract] [Full Text] [PDF]
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T. Lechler, G. A. Jonsdottir, S. K. Klee, D. Pellman, and R. Li A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast J. Cell Biol., October 15, 2001; 155(2): 261 - 270. [Abstract] [Full Text] [PDF]
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