HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 43, 41573-41576, October 24, 2003

This Article Full Text (PDF) All Versions of this Article: 278/43/41573    most recent R300026200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Donaldson, J. G. Search for Related Content PubMed PubMed Citation Articles by Donaldson, J. G. Social Bookmarking                      What's this?

Minireview

Multiple Roles for Arf6: Sorting, Structuring, and Signaling at the Plasma Membrane^*

Julie G. Donaldson

From the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

	INTRODUCTION

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
The ADP-ribosylation factors (Arfs)¹ are a family of Ras-related, low molecular mass (20 kDa), GTP-binding proteins that are expressed in all eukaryotes. There are six mammalian Arfs and many more Arf-like proteins. Like all GTPases, Arfs cycle between GDP-bound, inactive and GTP-bound, active states. In the active state, Arfs interact with proteins and other effector molecules to carry out their functions. Although Arf1 and its activities at the Golgi complex have been extensively studied, Arf6 has been the subject of increased attention over the past 5 years. Arf6 influences membrane trafficking and the actin cytoskeleton at the plasma membrane (PM). The goal of this review is to summarize these recent findings and provide a cellular context for understanding Arf6 function.

There are homologues of mammalian Arf6 in almost all eukaryotes including Xenopus laevis (97% amino acid sequence identity), Drosophila melanogaster (97%), Caenorhabditis elegans (88%), Schizosaccharomyces pombe (75%), and Saccharomyces cerevisiae (60%). All Arfs are N-terminally myristoylated, and all Arf6 homologues are basic proteins with predicted pIs in the range of 8.5–9.5. It is this characteristic and a signature dipeptide sequence (Gln-Ser) (1) adjacent to the effector domain interaction site, Switch I, that allow homologues of Arf6 to be identified. By contrast, other Arf isoforms have predicted pIs in the range of 6.0–7.0. It is likely that its positive surface charge and N-terminal myristoylation target Arf6 to the plasma membrane. This may explain why, during the GTPase cycle, Arf6-GDP, unlike Arf1-GDP, is retained on membranes to a large extent (2, 3) although release of Arf6-GDP to the cytosol cannot be ruled out (4). The absence of an Arf6 homologue in Arabadopsis or other plant species suggests that Arf6 is not present in plants.

Arf6 activation and inactivation are catalyzed by guanine nucleotide exchange factors (GEFs) that facilitate GTP binding and GTPase-activating proteins (GAPs) that catalyze GTP hydrolysis. In general, Arf6 GEFs are not inhibited by the fungal metabolite brefeldin A, in contrast with other Arf GEFs (5). The ARNO/cytohesin and EFA6 families of Arf6 GEFs contain a catalytic Sec7 homology domain and a pleckstrin homology domain thought to be involved in membrane targeting (5). Arf-GEP100, another Arf6-specific GEF, also contains an IQ motif and localizes to endosomal membranes (6). Candidate Arf6 GAPs are even more plentiful. These multidomain proteins can contain, in addition to the Arf GAP domain, pleckstrin homology, Src homology 2 and 3, and proline-rich domains capable of interacting with a multitude of signaling molecules that impact the actin cytoskeleton. As these regulators will not be further discussed, the reader is referred to two reviews in this area (5, 7).

The molecular structures of both GDP- and GTP-bound Arf6 have been published, and the differences and similarities with the Arf1 structures provide some insight into mechanisms of activation and interaction with effector proteins (8). The effector domain regions, Switch I and Switch II, are mostly identical in Arf6 and Arf1 and hence the two Arfs may share many interacting proteins. However, the glutamine and serine residues unique to Arf6 have been shown to confer distinct guanine nucleotide binding properties on Arf6 (9) and to be required for the actin rearrangement activities of Arf6 observed in cells (1). Mutations of these two residues and others in the effector domain of Arf6 will be useful for sorting out Arf6-specific functions. For example, expression of Arf6 (T175A), a rapidly cycling Arf6 mutant (based on a similar mutation in Ras), caused increased PM ruffling and cell migration (10). Additionally, Arf6 mutants defective in GTP binding (T27N) and GTP hydrolysis (Q67L) have been used to identify locations where active Arf6 is needed and to define the consequences of constitutively active Arf6, respectively. However, observations obtained with these inactive and active mutants should be interpreted with caution as Arf6 function normally depends on its GTPase cycle, and expression of any mutant that blocks the cycle may block Arf6 function (see below). By contrast, exogenous expression of wild type Arf6 has no discernible effect on cells in most cases (3).

The many cellular functions ascribed to Arf6 indicate that the activities of Arf6 at the PM are complex. It is likely that Arf6 gets activated and inactivated at many locations along the PM where it can influence the sorting of membrane proteins, endocytic pathways, and the structure of the plasma membrane (Fig. 1). This is reminiscent of Arf1 function at the Golgi complex where multiple sites of action of Arf1 influence many membrane trafficking steps into and out of the Golgi and the structure of the Golgi complex.

View larger version (20K): [in this window] [in a new window]   FIG. 1. Multiple sites of action of Arf6. Filled green circles, Arf6-GTP; open green circles, Arf6-GDP; black, membranes with PIP2; blue, other membranes. Note multiple sites of activation and inactivation of Arf6 along the PM. Activation of Arf6 can lead to: A, effects on cortical actin leading to protrusions, ruffling, cell spreading, cell migration, wound healing, and cell/tissue differentiation. B, stimulated endocytosis (macropinocytosis) during formation of protrusions and rapid membrane recycling of membrane back to the PM. C, turnover of adherens junction proteins by their endocytosis in polarized epithelial cells at the onset of cell migration/wound healing. D, the constitutive endocytosis of membrane proteins into Arf6 endosomes does not, per se, require Arf6 activity. However, GTP hydrolysis on Arf6 (by GAP) is required for the recycling of membrane back to the PM and for convergence with clathrin cargo-containing, Rab5-associated early endosomes. Expression of constitutively active Arf6 (Arf6Q67L) causes fusion of Arf6 early endosomes and blocks both recycling and convergence (red arrow). E, activation of Arf6 can stimulate release of regulated secretory granule exocytosis. F, priming the PM for the formation of clathrin-coated pits and sorting receptors at the PM, including G protein-coupled receptors (GPCR) into clathrin-coated pits and CPE for internalization.

Arfs are thought to act through 1) the recruitment of cytosolic coat proteins onto membranes to facilitate sorting and vesicle formation, 2) the activation of lipid-modifying enzymes, and 3) the modulation of actin structures. The ability of active Arf1 to recruit a variety of cytosolic coat proteins onto Golgi membranes is well documented in vitro and in cells (11). By contrast, there are as yet no identified coat proteins that are recruited to membranes by active Arf6, although the binding of Arf6-GTP to adaptor protein 1 and other cytosolic coat proteins has been demonstrated in vitro (12, 13). Rather, Arf6 is more closely associated with membrane lipid modifications and modulation of the actin cytoskeleton (Fig. 2).

View larger version (20K): [in this window] [in a new window]   FIG. 2. Proteins and pathways affected by Arf6. Refer to text. Green arrows denote stimulation. Blue arrows denote an influence of Rac-GTP, PIP2, and PA on actin structures and membrane traffic.

Although all Arfs activate phosphatidylinositol 4-phosphate 5-kinase (PIP5-kinase) in vitro, in cells it is Arf6 that localizes with, and activates, PIP5-kinase (14). PIP5-kinase is responsible for generating phosphatidylinositol 4,5-bisphosphate (PIP₂), a major PM phosphoinositide involved in membrane traffic and actin rearrangements (15, 16). Therefore, this has provided a key to understanding cellular activities of Arf6. Furthermore, a biophysical study demonstrating that Arf6 binding to PIP₂ vesicles alters bilayer structure (17) suggests another way that Arf6 might affect membrane structure. Arfs also activate phospholipase D (PLD), an enzyme that hydrolyzes phosphatidylcholine to produce phosphatidic acid (PA), and in cells, PLD1 is activated by many agonists. Although the intracellular mediators in the pathway are not clear, accumulating evidence implicates Arf6, as it can directly bind to and activate PLD (18, 19) leading to regulated secretion (20), stimulated membrane ruffling (21), and other consequences associated with PLD activity (22). Because PA can also activate PIP5-kinase, regulation of both PLD and PIP5-kinase by Arf6 can greatly amplify a PIP₂-mediated signal (Fig. 2). Thus, changes in membrane lipid composition and structure may mediate Arf6 alterations of the cortical actin cytoskeleton and regulation of membrane traffic and signal transduction.

	Arf6 and Actin

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
The ability of Arf6 to affect the cortical actin cytoskeleton, cell shape, and cell migration is now well recognized (Fig. 1A). In 1996, however, it was unexpected to find that an Arf protein could, upon activation, generate protrusive structures (23). These observations were later extended to include a requirement for Arf6 activity for cell spreading (3), Rac-induced ruffling (24, 25), cell migration (26–28), wound healing (27), and Fc-mediated phagocytosis (29, 30). The requirement was demonstrated by inhibition of these activities upon expression of the GTP-binding defective, dominant negative mutant of Arf6, T27N, and in some cases by the stimulation of these activities by overexpression of an Arf6 GEF (27, 31, 32). It is important to note, however, that expression of Arf6Q67L, the constitutively active mutant, generally blocks all of the above actin activities (29, 32), consistent with the requirement that Arf6 cycles between active and inactive forms to function properly.

In many cases it appears that Arf6 changes the actin structure at the PM through activation of Rac, the Rho protein implicated in membrane ruffling. Arf6 is required for and enhances the ability of Rac to form PM ruffles (24). Furthermore, expression of an Arf6-specific GEF, EFA6, in cells generates protrusions and ruffles through activation of Arf6 (31, 32) and this activity appears to require Rac activation downstream of Arf6 activation (31). Indeed, direct evidence that Arf6-GTP leads to activation of Rac has been obtained (27), although the mechanism has not been identified. Interestingly, both Arf6 and Rac bind to a common effector protein Arfaptin 2/Partner of Rac (33). Unfortunately, the function of Arfaptin 2 is not known, and it may show more specificity for Arf1 (34). Another identified partner of Arf6, Arfophilin, appears to be more selective for Arf6 than for Arf1 (34). This protein binds to Switch I and II regions of Arf6 but recognizes the N-terminal portion of Arf5 (34). Intriguingly, Arfophilin is identical to a Rab11 effector protein, FIP3, suggesting common effectors that might bridge Arf6 and Rab11 functions (35).

The effects of Arf6 on membrane lipid composition can also lead to changes in cortical actin cytoskeleton, perhaps working synergistically with activation of Rac. Phosphoinositides, and in particular, PIP₂, can recruit and influence the activity of a number of actin-binding proteins that lead to changes in the cortical actin network (see Ref. 16 for review). PIP₂, PIP5-kinase, and Arf6 are present together on the PM and endosomal membranes. Acute stimulation of Arf6 activation leads to protrusions of PIP₂-rich PM driven by actin polymerization (14, 32) and stimulated membrane internalization and rapid recycling of the membrane back to the PM (32) (Fig. 1B). At low expression levels, PIP5-kinase and Arf6 act synergistically to form protrusions (32), and in CHO cells expression of either Arf6Q67L or PIP5-kinase generates actin comet-propelled endosomal membranes (36).

	Arf6 and Cell Polarity

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
Recent reports have implicated Arf6 in determining polarized structures in neuronal cells and in yeast and in the disassembly of polarized epithelium. Arf6 can regulate dendritic branching in hippocampal neurons (37) and neurite outgrowth in PC12 cells (38). In yeast, the Arf6 homologue, Arf3, localizes to the growing bud and is important for polarized growth and bud site selection (39).

The stimulation of migration of MDCK cells in response to growth factor (26, 40) or during wound healing (27) involves the transition from an epithelium with cells held together by adhesive interactions to more motile cells freed of these adhesions (Fig. 1C). The transformation and conversion to a motile cell required the activation of Arf6, as these processes were inhibited by expression of Arf6T27N (26, 27). In response to hepatocyte growth factor (HGF), Arf6 is continuously activated whereas Rac is initially inactivated, leading to the internalization of adherens junction proteins (40). Active Arf6 binds to Nm23-H1, a nucleoside diphosphate kinase that has been implicated in both the inhibition of Rac activation and dynamin-dependent endocytosis, and could account for the observations at early times of HGF treatment (41). At later times, levels of Rac-GTP increase and the cells begin to scatter (40). Another study demonstrated that the activation of Arf6 induced by expression of ARNO, an Arf6 GEF, could initiate cell migration in the absence of HGF stimulation and enhance wound healing in MDCK cells (27). The activation of Arf6 led to two downstream effects, one involving Rac activation and one involving PLD (27). Although PLD activity was not required for the activation of Rac, both the Rac and PLD pathway were required for the stimulation of cell migration (27). In addition to roles in stimulating migration of epithelial cells, Arf6 is also required in leukocytes for chemokine-stimulated migration across endothelial cells (28).

	Arf6 and Membrane Traffic

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
It is difficult to describe Arf6 actions on cell morphology, polarity, and the actin cytoskeleton without including its effects on membrane traffic. In addition to its PM localization, Arf6 is associated with endosomal membranes in many cells (42). In kidney proximal tubules, Arf6 localizes to specialized apical endosomes (43), and in CHO cells there is partial overlap between Arf6-associated endosomes and endosomes containing the transferrin receptor (44). In HeLa and other types of epithelial cells, Arf6 is associated with a distinct endosomal compartment that contains integral membrane proteins that are endocytosed into cells independently of adaptor protein 2 and clathrin (45, 46). This separate endosomal system that exists in parallel with the classical, transferrin-containing endosomal system is depicted in Fig. 1D and is the trafficking route followed by a number of PM proteins including the major histocompatibility complex class I proteins (MHCI) (45, 46), integrins (32), and E-cadherin (47). After internalization, these proteins can either recycle back to the PM (45, 48) or fuse with the Rab5-associated endosomal system (46). The crossover from the Arf6 endosome to the Rab5 endosome is apparently a trafficking route followed by the M2-muscarinic acetylcholine receptor (49) and may be part of the mechanism for the down-regulation of surface MHCI induced by Nef, an HIV-encoded protein (50). Nef stimulates the activation of Arf6, enhances endocytosis of MHCI, inhibits MHCI recycling, and causes MHCI to traffic to the Golgi complex, presumably from the Rab5 early endosome (50).

Although Arf6 is associated with these endosomal membranes in HeLa cells, Arf6 activation is not required for internalization and trafficking through this pathway. Inactivation of Arf6, however, is a requirement. When Arf6 activation is stimulated and protrusions form, increased membrane is taken up by macropinocytosis and then recycled back to the PM, provided that Arf6 can be inactivated by GAP (32). If, however, Arf6Q67L is overexpressed, membrane is internalized but not recycled, and cells accumulate PIP₂ and F-actin-coated endosomal structures (Fig. 1D) that contain only clathrin-independent cargo proteins such as MHCI (32, 46). Expression of the peripheral myelin protein, Pmp22, in HeLa cells appears to activate Arf6 and induces the formation of similar endocytic structures (51), suggesting a role for Arf6 in the formation of the myelin sheath, a process that is poorly understood.

Another membrane trafficking function attributed to Arf6 is its role in certain regulated secretory events (Fig. 1E). In PC12 cells, Arf6 is associated with the dense core granules that are docked at the PM (52), and upon calcium stimulation, Arf6 is activated and increases PLD activity resulting in membrane fusion (20, 53). Expression of a mutant of Arf6 (N48I) that cannot activate PLD inhibits secretion, demonstrating that activation of PLD is a major downstream effect of Arf6 that leads to secretion (53). In another example, stimulation of adipocytes with endothelin acts via G_q to release a pool of Glut4-containing vesicles, but expression of Arf6T27N blocks this release (54, 55). A recent study examining the role of Arf6 in Fc-mediated phagocytosis found that vesicles accumulated in cells expressing Arf6T27N, suggesting that activation of Arf6 leads to the exocytosis of vesicles required to complete phagocytosis (30).

	Arf6 at the PM: Priming and Sorting Functions

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
In addition to its effects on cortical actin and clathrin-independent endocytosis, Arf6 regulation of PIP₂ synthesis can influence other PM activities (Fig. 1F). PIP₂ is required for the recruitment of AP2/clathrin onto forming clathrin-coated pits but is rapidly lost upon vesicle fission. A recent study demonstrated that Arf6Q67L binds to PIP5-kinase I-, activates the kinase, and leads to enhanced AP2/clathrin binding to a synaptic vesicle membrane preparation (56). Interestingly, an earlier study reported an effect of expression of Arf6 mutants on the morphology of clathrin-coated pits at the apical surface of MDCK cells (57).

Two areas of investigation have uncovered roles for Arf6 in sorting of PM proteins to facilitate their internalization. The agonist-induced down-regulation of ₂-adrenergic and luteinizing hormone receptors requires Arf6 activity. In both cases, engagement of the receptor leads to activation of Arf6 (58, 59) facilitating the release of sequestered arrestin to allow internalization via clathrin-mediated endocytosis (60). Yet another role for Arf6 involves the transmembrane form of carboxypeptidase E (CPE), a sorting receptor for regulated secretory granules that, after secretion, is recycled back to the Golgi complex. This form of CPE extends about 6 amino acid residues (SETLNF) into the cytoplasm and interacts specifically with Arf6-GTP (61). Remarkably, expression of Arf6-T27N blocks the recycling of CPE from the PM back to the Golgi, and mutation of the six residues in CPE important for Arf6 binding also inhibits recycling (61).

	Concluding Remarks

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 
Although we are beginning to understand the breadth of Arf6 activities, the identification of more proteins that interact with Arf6 is needed to develop a molecular framework for understanding Arf6 function. The multiple sites of action of Arf6 at the PM highlight the importance of spatial and temporal regulation of Arf6 by connecting to specific GEFs, GAPs, and effectors. Although Arf6 may act in a constitutive capacity in resting cells, it is subject to acute stimulation through signal transduction pathways. Further studies on Arf6 function will shed light on the complex interplay between signal transduction, membrane traffic, and the cytoskeleton.

	FOOTNOTES

 
^* This minireview will be reprinted in the 2003 Minireview Compendium, which will be available in January, 2004.

To whom correspondence should be addressed: Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bldg. 50, Rm. 2503, Bethesda, MD 20892. Tel.: 301-402-2907; Fax: 301-402-1519; E-mail: jdonalds{at}helix.nih.gov.

¹ The abbreviations used are: Arf, ADP-ribosylation factor; PM, plasma membrane; GEF, guanine nucleotide exchange factor; GAP, GTPase-activating protein; PIP5-kinase, phosphatidylinositol 4-phosphate 5-kinase; PIP₂, phosphatidylinositol 4,5-bisphosphate; CHO, Chinese hamster ovary; MDCK, Madin-Darby canine kidney; PLD, phospholipase D; HIV, human immunodeficiency virus; PA, phosphatidic acid; HGF, hepatocyte growth factor; CPE, carboxypeptidase E; MHCI, major histocompatibility complex class I.

	ACKNOWLEDGMENTS

 
I thank Rob Donaldson, Cathy Jackson, Ed Korn, and members of my laboratory for comments on the manuscript.

	REFERENCES

TOP INTRODUCTION Arf6 and Actin Arf6 and Cell Polarity Arf6 and Membrane Traffic Arf6 at the PM:... Concluding Remarks REFERENCES

 

1. Al-Awar, O., Radhakrishna, H., Powell, N. N., and Donaldson, J. G. (2000) Mol. Cell. Biol. 20, 5998–6007[Abstract/Free Full Text]
2. Cavenagh, M. M., Whitney, J. A., Carroll, K., Zhang, C., Boman, A. L., Rosenwald, A. G., Mellman, I., and Kahn, R. A. (1996) J. Biol. Chem. 271, 21767–21774[Abstract/Free Full Text]
3. Song, J., Khachikian, Z., Radhakrishna, H., and Donaldson, J. G. (1998) J. Cell Sci. 111, 2257–2267[Abstract]
4. Gaschet, J., and Hsu, V. W. (1999) J. Biol. Chem. 274, 20040–20045[Abstract/Free Full Text]
5. Jackson, C. L., and Casanova, J. E. (2000) Trends Cell Biol. 10, 60–67[CrossRef][Medline] [Order article via Infotrieve]
6. Someya, A., Sata, M., Takeda, K., Pacheco-Rodriguez, G., Ferrans, V. J., Moss, J., and Vaughan, M. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 2413–2418[Abstract/Free Full Text]
7. Jackson, T. R., Kearns, B. G., and Theibert, A. B. (2000) Trends Biochem. Sci. 25, 489–495[CrossRef][Medline] [Order article via Infotrieve]
8. Pasqualato, S., Menetrey, J., Franco, M., and Cherfils, J. (2001) EMBO Rep. 2, 234–238[CrossRef][Medline] [Order article via Infotrieve]
9. Menetrey, J., Macia, E., Pasqualato, S., Franco, M., and Cherfils, J. (2000) Nat. Struct. Biol. 7, 466–469[CrossRef][Medline] [Order article via Infotrieve]
10. Santy, L. C. (2002) J. Biol. Chem. 277, 40185–40188[Abstract/Free Full Text]
11. Donaldson, J. G., and Jackson, C. L. (2000) Curr. Opin. Cell Biol. 12, 475–482[CrossRef][Medline] [Order article via Infotrieve]
12. Austin, C., Boehm, M., and Tooze, S. A. (2002) Biochemistry 41, 4669–4677[CrossRef][Medline] [Order article via Infotrieve]
13. Takatsu, H., Yoshino, K., Toda, K., and Nakayama, K. (2002) Biochem. J. 365, 369–378[CrossRef][Medline] [Order article via Infotrieve]
14. Honda, A., Nogami, M., Yokozeki, T., Yamazaki, M., Nakamura, H., Watanabe, H., Kawamoto, K., Nakayama, K., Morris, A. J., Frohman, M. A., and Kanaho, Y. (1999) Cell 99, 521–532[CrossRef][Medline] [Order article via Infotrieve]
15. Czech, M. P. (2003) Annu. Rev. Physiol. 65, 791–815[CrossRef][Medline] [Order article via Infotrieve]
16. Yin, H. L., and Janmey, P. A. (2003) Annu. Rev. Physiol. 65, 761–789[CrossRef][Medline] [Order article via Infotrieve]
17. Ge, M., Cohen, J. S., Brown, H. A., and Freed, J. H. (2001) Biophys. J. 81, 994–1005[Medline] [Order article via Infotrieve]
18. Melendez, A. J., Harnett, M. M., and Allen, J. M. (2001) Curr. Biol. 11, 869–874[CrossRef][Medline] [Order article via Infotrieve]
19. Powner, D. J., Hodgkin, M. N., and Wakelam, M. J. (2002) Mol. Biol. Cell 13, 1252–1262[Abstract/Free Full Text]
20. Caumont, A. S., Galas, M. C., Vitale, N., Aunis, D., and Bader, M. F. (1998) J. Biol. Chem. 273, 1373–1379[Abstract/Free Full Text]
21. O'Luanaigh, N., Pardo, R., Fensome, A., Allen-Baume, V., Jones, D., Holt, M. R., and Cockcroft, S. (2002) Mol. Biol. Cell 13, 3730–3746[Abstract/Free Full Text]
22. Dana, R. R., Eigsti, C., Holmes, K. L., and Leto, T. L. (2000) J. Biol. Chem. 275, 32566–32571[Abstract/Free Full Text]
23. Radhakrishna, H., Klausner, R. D., and Donaldson, J. G. (1996) J. Cell Biol. 134, 935–947[Abstract/Free Full Text]
24. Radhakrishna, H., Al-Awar, O., Khachikian, Z., and Donaldson, J. G. (1999) J. Cell Sci. 112, 855–866[Abstract]
25. Boshans, R. L., Szanto, S., van Aelst, L., and D'Souza-Schorey, C. (2000) Mol. Cell. Biol. 20, 3685–3694[Abstract/Free Full Text]
26. Palacios, F., Price, L., Schweitzer, J., Collard, J. G., and D'Souza-Schorey, C. (2001) EMBO J. 20, 4973–4986[CrossRef][Medline] [Order article via Infotrieve]
27. Santy, L. C., and Casanova, J. E. (2001) J. Cell Biol. 154, 599–610[Abstract/Free Full Text]
28. Weber, K. S., Weber, C., Ostermann, G., Dierks, H., Nagel, W., and Kolanus, W. (2001) Curr. Biol. 11, 1969–1974[CrossRef][Medline] [Order article via Infotrieve]
29. Zhang, Q., Cox, D., Tseng, C. C., Donaldson, J. G., and Greenberg, S. (1998) J. Biol. Chem. 273, 19977–19981[Abstract/Free Full Text]
30. Niedergang, F., Colucci-Guyon, E., Dubois, T., Raposo, G., and Chavrier, P. (2003) J. Cell Biol. 161, 1143–1150[Abstract/Free Full Text]
31. Franco, M., Peters, P. J., Boretto, J., van Donselaar, E., Neri, A., D'Souza-Schorey, C., and Chavrier, P. (1999) EMBO J. 18, 1480–1491[CrossRef][Medline] [Order article via Infotrieve]
32. Brown, F. D., Rozelle, A. L., Yin, H. L., Balla, T., and Donaldson, J. G. (2001) J. Cell Biol. 154, 1007–1017[Abstract/Free Full Text]
33. D'Souza-Schorey, C., Boshans, R. L., McDonough, M., Stahl, P. D., and Van Aelst, L. (1997) EMBO J. 16, 5445–5454[CrossRef][Medline] [Order article via Infotrieve]
34. Shin, O. H., Couvillon, A. D., and Exton, J. H. (2001) Biochemistry 40, 10846–10852[CrossRef][Medline] [Order article via Infotrieve]
35. Hickson, G. R., Matheson, J., Riggs, B., Maier, V. H., Fielding, A. B., Prekeris, R., Sullivan, W., Barr, F. A., and Gould, G. W. (2003) Mol. Biol. Cell 14, 2908–2920[Abstract/Free Full Text]
36. Schafer, D. A., D'Souza-Schorey, C., and Cooper, J. A. (2000) Traffic 1, 892–903[Medline] [Order article via Infotrieve]
37. Hernandez-Deviez, D. J., Casanova, J. E., and Wilson, J. M. (2002) Nat. Neurosci. 5, 623–624[Medline] [Order article via Infotrieve]
38. Albertinazzi, C., Za, L., Paris, S., and De Curtis, I. (2003) Mol. Biol. Cell 14, 1295–1307[Abstract/Free Full Text]
39. Huang, C. F., Liu, Y. W., Tung, L., Lin, C. H., and Lee, F. J. (2003) Mol. Biol. Cell DOI 10.1091/mbc.03-01-0013
40. Palacios, F., and D'Souza-Schorey, C. (2003) J. Biol. Chem. 278, 17395–17400[Abstract/Free Full Text]
41. Palacios, F., Schweitzer, J. K., Boshans, R. L., and D'Souza-Schorey, C. (2002) Nat. Cell Biol. 4, 929–936[CrossRef][Medline] [Order article via Infotrieve]
42. Peters, P. J., Hsu, V. W., Ooi, C. E., Finazzi, D., Teal, S. B., Oorschot, V., Donaldson, J. G., and Klausner, R. D. (1995) J. Cell Biol. 128, 1003–1017[Abstract/Free Full Text]
43. Maranda, B., Brown, D., Bourgoin, S., Casanova, J. E., Vinay, P., Ausiello, D. A., and Marshansky, V. (2001) J. Biol. Chem. 276, 18540–18550[Abstract/Free Full Text]
44. D'Souza-Schorey, C., van Donselaar, E., Hsu, V. W., Yang, C., Stahl, P. D., and Peters, P. J. (1998) J. Cell Biol. 140, 603–616[Abstract/Free Full Text]
45. Radhakrishna, H., and Donaldson, J. G. (1997) J. Cell Biol. 139, 49–61[Abstract/Free Full Text]
46. Naslavsky, N., Weigert, R., and Donaldson, J. G. (2003) Mol. Biol. Cell 14, 417–431[Abstract/Free Full Text]
47. Paterson, A. D., Parton, R. G., Ferguson, C., Stow, J. L., and Yap, A. S. (2003) J. Biol. Chem. 278, 21050–21057[Abstract/Free Full Text]
48. Caplan, S., Naslavsky, N., Hartnell, L. M., Lodge, R., Polishchuk, R. S., Donaldson, J. G., and Bonifacino, J. S. (2002) EMBO J. 21, 2557–2567[CrossRef][Medline] [Order article via Infotrieve]
49. Delaney, K. A., Murph, M. M., Brown, L. M., and Radhakrishna, H. (2002) J. Biol. Chem. 277, 33439–33446[Abstract/Free Full Text]
50. Blagoveshchenskaya, A. D., Thomas, L., Feliciangeli, S. F., Hung, C. H., and Thomas, G. (2002) Cell 111, 853–866[CrossRef][Medline] [Order article via Infotrieve]
51. Chies, R., Nobbio, L., Edomi, P., Schenone, A., Schneider, C., and Brancolini, C. (2003) J. Cell Sci. 116, 987–999[Abstract/Free Full Text]
52. Galas, M. C., Helms, J. B., Vitale, N., Thierse, D., Aunis, D., and Bader, M. F. (1997) J. Biol. Chem. 272, 2788–2793[Abstract/Free Full Text]
53. Vitale, N., Chasserot-Golaz, S., Bailly, Y., Morinaga, N., Frohman, M. A., and Bader, M. F. (2002) J. Cell Biol. 159, 79–89[Abstract/Free Full Text]
54. Bose, A., Cherniack, A. D., Langille, S. E., Nicoloro, S. M., Buxton, J. M., Park, J. G., Chawla, A., and Czech, M. P. (2001) Mol. Cell. Biol. 21, 5262–5275[Abstract/Free Full Text]
55. Lawrence, J. T., and Birnbaum, M. J. (2001) Mol. Cell. Biol. 21, 5276–5285[Abstract/Free Full Text]
56. Krauss, M., Kinuta, M., Wenk, M. R., De Camilli, P., Takei, K., and Haucke, V. (2003) J. Cell Biol. 162, 113–124[Abstract/Free Full Text]
57. Altschuler, Y., Liu, S., Katz, L., Tang, K., Hardy, S., Brodsky, F., Apodaca, G., and Mostov, K. (1999) J. Cell Biol. 147, 7–12[Abstract/Free Full Text]
58. Salvador, L. M., Mukherjee, S., Kahn, R. A., Lamm, M. L., Fazleabas, A. T., Maizels, E. T., Bader, M. F., Hamm, H., Rasenick, M. M., Casanova, J. E., and Hunzicker-Dunn, M. (2001) J. Biol. Chem. 276, 33773–33781[Abstract/Free Full Text]
59. Claing, A., Chen, W., Miller, W. E., Vitale, N., Moss, J., Premont, R. T., and Lefkowitz, R. J. (2001) J. Biol. Chem. 276, 42509–42513[Abstract/Free Full Text]
60. Mukherjee, S., Gurevich, V. V., Preninger, A., Hamm, H. E., Bader, M. F., Fazleabas, A. T., Birnbaumer, L., and Hunzicker-Dunn, M. (2002) J. Biol. Chem. 277, 17916–17927[Abstract/Free Full Text]
61. Arnaoutova, I., Jackson, C. L., Al-Awar, O., Donaldson, J. G., and Loh, Y. P. (2003) Mol. Biol. Cell DOI 10.1091/mbc.02-11-0758

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				C. Sironi, T. Teesalu, A. Muggia, G. Fontana, F. Marino, S. Savaresi, and D. Talarico EFA6A encodes two isoforms with distinct biological activities in neuronal cells J. Cell Sci., June 15, 2009; 122(12): 2108 - 2118. [Abstract] [Full Text] [PDF]

				R. Puertollano and K. Kiselyov TRPMLs: in sickness and in health Am J Physiol Renal Physiol, June 1, 2009; 296(6): F1245 - F1254. [Abstract] [Full Text] [PDF]

				G. H. Diering, J. Church, and M. Numata Secretory Carrier Membrane Protein 2 Regulates Cell-surface Targeting of Brain-enriched Na+/H+ Exchanger NHE5 J. Biol. Chem., May 15, 2009; 284(20): 13892 - 13903. [Abstract] [Full Text] [PDF]

				S. Nawaz, A. Kippert, A. S. Saab, H. B. Werner, T. Lang, K.-A. Nave, and M. Simons Phosphatidylinositol 4,5-Bisphosphate-Dependent Interaction of Myelin Basic Protein with the Plasma Membrane in Oligodendroglial Cells and Its Rapid Perturbation by Elevated Calcium J. Neurosci., April 15, 2009; 29(15): 4794 - 4807. [Abstract] [Full Text] [PDF]

				D. Marchant, A. Sall, X. Si, T. Abraham, W. Wu, Z. Luo, T. Petersen, R. G. Hegele, and B. M. McManus ERK MAP kinase-activated Arf6 trafficking directs coxsackievirus type B3 into an unproductive compartment during virus host-cell entry J. Gen. Virol., April 1, 2009; 90(4): 854 - 862. [Abstract] [Full Text] [PDF]

				K. Miura, J.-M. Nam, C. Kojima, N. Mochizuki, and H. Sabe EphA2 Engages Git1 to Suppress Arf6 Activity Modulating Epithelial Cell-Cell Contacts Mol. Biol. Cell, April 1, 2009; 20(7): 1949 - 1959. [Abstract] [Full Text] [PDF]

				V. Muralidharan-Chari, H. Hoover, J. Clancy, J. Schweitzer, M. A. Suckow, V. Schroeder, F. J. Castellino, J. S. Schorey, and C. D'Souza-Schorey ADP-Ribosylation Factor 6 Regulates Tumorigenic and Invasive Properties In vivo Cancer Res., March 15, 2009; 69(6): 2201 - 2209. [Abstract] [Full Text] [PDF]

				A. Begle, P. Tryoen-Toth, J. de Barry, M.-F. Bader, and N. Vitale ARF6 Regulates the Synthesis of Fusogenic Lipids for Calcium-regulated Exocytosis in Neuroendocrine Cells J. Biol. Chem., February 20, 2009; 284(8): 4836 - 4845. [Abstract] [Full Text] [PDF]

				B. Hu, B. Shi, M. J. Jarzynka, J.-J. Yiin, C. D'Souza-Schorey, and S.-Y. Cheng ADP-Ribosylation Factor 6 Regulates Glioma Cell Invasion through the IQ-Domain GTPase-Activating Protein 1-Rac1-Mediated Pathway Cancer Res., February 1, 2009; 69(3): 794 - 801. [Abstract] [Full Text] [PDF]

				A. W. Lau and M. M. Chou The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway J. Cell Sci., December 15, 2008; 121(24): 4008 - 4017. [Abstract] [Full Text] [PDF]

				P.-C. Tsai, S.-W. Lee, Y.-W. Liu, C.-W. Chu, K.-Y. Chen, J.-C. Ho, and F.-J. S. Lee Afi1p Functions as an Arf3p Polarization-specific Docking Factor for Development of Polarity J. Biol. Chem., June 13, 2008; 283(24): 16915 - 16927. [Abstract] [Full Text] [PDF]

				V. L. Ha, S. Bharti, H. Inoue, W. C. Vass, F. Campa, Z. Nie, A. de Gramont, Y. Ward, and P. A. Randazzo ASAP3 Is a Focal Adhesion-associated Arf GAP That Functions in Cell Migration and Invasion J. Biol. Chem., May 30, 2008; 283(22): 14915 - 14926. [Abstract] [Full Text] [PDF]

				E. Walseng, O. Bakke, and P. A. Roche Major Histocompatibility Complex Class II-Peptide Complexes Internalize Using a Clathrin- and Dynamin-independent Endocytosis Pathway J. Biol. Chem., May 23, 2008; 283(21): 14717 - 14727. [Abstract] [Full Text] [PDF]

				Z. A. Karim, W. Choi, and S. W. Whiteheart Primary Platelet Signaling Cascades and Integrin-mediated Signaling Control ADP-ribosylation Factor (Arf) 6-GTP Levels during Platelet Activation and Aggregation J. Biol. Chem., May 2, 2008; 283(18): 11995 - 12003. [Abstract] [Full Text] [PDF]

				K. Haberg, R. Lundmark, and S. R. Carlsson SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking J. Cell Sci., May 1, 2008; 121(9): 1495 - 1505. [Abstract] [Full Text] [PDF]

				V. Kolsch, P. G. Charest, and R. A. Firtel The regulation of cell motility and chemotaxis by phospholipid signaling J. Cell Sci., March 1, 2008; 121(5): 551 - 559. [Abstract] [Full Text] [PDF]

				H. Yano, I. Kobayashi, Y. Onodera, F. Luton, M. Franco, Y. Mazaki, S. Hashimoto, K. Iwai, Z. Ronai, and H. Sabe Fbx8 Makes Arf6 Refractory to Function via Ubiquitination Mol. Biol. Cell, March 1, 2008; 19(3): 822 - 832. [Abstract] [Full Text] [PDF]

				P. Uawithya, T. Pisitkun, B. E. Ruttenberg, and M. A. Knepper Transcriptional profiling of native inner medullary collecting duct cells from rat kidney Physiol Genomics, January 17, 2008; 32(2): 229 - 253. [Abstract] [Full Text] [PDF]

				B. E. Richardson, K. Beckett, S. J. Nowak, and M. K. Baylies SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling at the site of myoblast fusion Development, December 15, 2007; 134(24): 4357 - 4367. [Abstract] [Full Text] [PDF]

				V. Braun, C. Deschamps, G. Raposo, P. Benaroch, A. Benmerah, P. Chavrier, and F. Niedergang AP-1 and ARF1 Control Endosomal Dynamics at Sites of FcR mediated Phagocytosis Mol. Biol. Cell, December 1, 2007; 18(12): 4921 - 4931. [Abstract] [Full Text] [PDF]

				C.-C. Li, T.-C. Chiang, T.-S. Wu, G. Pacheco-Rodriguez, J. Moss, and F.-J. S. Lee ARL4D Recruits Cytohesin-2/ARNO to Modulate Actin Remodeling Mol. Biol. Cell, November 1, 2007; 18(11): 4420 - 4437. [Abstract] [Full Text] [PDF]

				J. A. Grodnitzky, N. Syed, M. J. Kimber, T. A. Day, J. G. Donaldson, and W. H. Hsu Somatostatin Receptors Signal through EFA6A-ARF6 to Activate Phospholipase D in Clonal beta-Cells J. Biol. Chem., May 4, 2007; 282(18): 13410 - 13418. [Abstract] [Full Text] [PDF]

				M. Sharma and B. R. Henderson IQ-domain GTPase-activating Protein 1 Regulates beta-Catenin at Membrane Ruffles and Its Role in Macropinocytosis of N-cadherin and Adenomatous Polyposis Coli J. Biol. Chem., March 16, 2007; 282(11): 8545 - 8556. [Abstract] [Full Text] [PDF]

				K. Venkateswarlu, K. G. Brandom, and H. Yun PI-3-kinase-dependent membrane recruitment of centaurin-{alpha}2 is essential for its effect on ARF6-mediated actin cytoskeleton reorganisation J. Cell Sci., March 1, 2007; 120(5): 792 - 801. [Abstract] [Full Text] [PDF]

				H. P. Price, M. Stark, and D. F. Smith Trypanosoma brucei ARF1 Plays a Central Role in Endocytosis and Golgi-Lysosome Trafficking Mol. Biol. Cell, March 1, 2007; 18(3): 864 - 873. [Abstract] [Full Text] [PDF]

				M. Cotton, P.-L. Boulay, T. Houndolo, N. Vitale, J. A. Pitcher, and A. Claing Endogenous ARF6 Interacts with Rac1 upon Angiotensin II Stimulation to Regulate Membrane Ruffling and Cell Migration Mol. Biol. Cell, February 1, 2007; 18(2): 501 - 511. [Abstract] [Full Text] [PDF]

				S. Breton and D. Brown New insights into the regulation of V-ATPase-dependent proton secretion Am J Physiol Renal Physiol, January 1, 2007; 292(1): F1 - F10. [Abstract] [Full Text] [PDF]

				H.-Y. Yoon, K. Miura, E. J. Cuthbert, K. K. Davis, B. Ahvazi, J. E. Casanova, and P. A. Randazzo ARAP2 effects on the actin cytoskeleton are dependent on Arf6-specific GTPase-activating-protein activity and binding to RhoA-GTP J. Cell Sci., November 15, 2006; 119(22): 4650 - 4666. [Abstract] [Full Text] [PDF]

				T. Shiba, H. Koga, H.-W. Shin, M. Kawasaki, R. Kato, K. Nakayama, and S. Wakatsuki Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1 PNAS, October 17, 2006; 103(42): 15416 - 15421. [Abstract] [Full Text] [PDF]

				A. Someya, J. Moss, and I. Nagaoka Involvement of a guanine nucleotide-exchange protein, ARF-GEP100/BRAG2a, in the apoptotic cell death of monocytic phagocytes J. Leukoc. Biol., October 1, 2006; 80(4): 915 - 921. [Abstract] [Full Text] [PDF]

				K. Singleton, N. Parvaze, K. R. Dama, K. S. Chen, P. Jennings, B. Purtic, M. D. Sjaastad, C. Gilpin, M. M. Davis, and C. Wulfing A Large T Cell Invagination with CD2 Enrichment Resets Receptor Engagement in the Immunological Synapse J. Immunol., October 1, 2006; 177(7): 4402 - 4413. [Abstract] [Full Text] [PDF]

				M. Krauss, V. Kukhtina, A. Pechstein, and V. Haucke Stimulation of phosphatidylinositol kinase type I-mediated phosphatidylinositol (4,5)-bisphosphate synthesis by AP-2{micro}-cargo complexes PNAS, August 8, 2006; 103(32): 11934 - 11939. [Abstract] [Full Text] [PDF]

				T. Suzuki, Y. Kanai, T. Hara, J. Sasaki, T. Sasaki, M. Kohara, T. Maehama, C. Taya, H. Shitara, H. Yonekawa, et al. Crucial Role of the Small GTPase ARF6 in Hepatic Cord Formation during Liver Development. Mol. Cell. Biol., August 1, 2006; 26(16): 6149 - 6156. [Abstract] [Full Text] [PDF]

				Z. Fang, Y. Miao, X. Ding, H. Deng, S. Liu, F. Wang, R. Zhou, C. Watson, C. Fu, Q. Hu, et al. Proteomic Identification and Functional Characterization of a Novel ARF6 GTPase-activating Protein, ACAP4 Mol. Cell. Proteomics, August 1, 2006; 5(8): 1437 - 1449. [Abstract] [Full Text] [PDF]

				M. Kalia, S. Kumari, R. Chadda, M. M. Hill, R. G. Parton, and S. Mayor Arf6-independent GPI-anchored Protein-enriched Early Endosomal Compartments Fuse with Sorting Endosomes via a Rab5/Phosphatidylinositol-3'-Kinase-dependent Machinery Mol. Biol. Cell, August 1, 2006; 17(8): 3689 - 3704. [Abstract] [Full Text] [PDF]

				T. Hiroi, A. Someya, W. Thompson, J. Moss, and M. Vaughan GEP100/BRAG2: Activator of ADP-ribosylation factor 6 for regulation of cell adhesion and actin cytoskeleton via E-cadherin and {alpha}-catenin PNAS, July 11, 2006; 103(28): 10672 - 10677. [Abstract] [Full Text] [PDF]

				L. Za, C. Albertinazzi, S. Paris, M. Gagliani, C. Tacchetti, and I. de Curtis {beta}PIX controls cell motility and neurite extension by regulating the distribution of GIT1 J. Cell Sci., July 1, 2006; 119(13): 2654 - 2666. [Abstract] [Full Text] [PDF]

				W. Natsume, K. Tanabe, S. Kon, N. Yoshida, T. Watanabe, T. Torii, and M. Satake SMAP2, a Novel ARF GTPase-activating Protein, Interacts with Clathrin and Clathrin Assembly Protein and Functions on the AP-1-positive Early Endosome/Trans-Golgi Network Mol. Biol. Cell, June 1, 2006; 17(6): 2592 - 2603. [Abstract] [Full Text] [PDF]

				M. Shmuel, L. C. Santy, S. Frank, D. Avrahami, J. E. Casanova, and Y. Altschuler ARNO through Its Coiled-coil Domain Regulates Endocytosis at the Apical Surface of Polarized Epithelial Cells J. Biol. Chem., May 12, 2006; 281(19): 13300 - 13308. [Abstract] [Full Text] [PDF]

				S. Klein, M. Franco, P. Chardin, and F. Luton Role of the Arf6 GDP/GTP Cycle and Arf6 GTPase-activating Proteins in Actin Remodeling and Intracellular Transport J. Biol. Chem., May 5, 2006; 281(18): 12352 - 12361. [Abstract] [Full Text] [PDF]

				S. Choi, J. Ko, J.-R. Lee, H. W. Lee, K. Kim, H. S. Chung, H. Kim, and E. Kim ARF6 and EFA6A regulate the development and maintenance of dendritic spines. J. Neurosci., May 3, 2006; 26(18): 4811 - 4819. [Abstract] [Full Text] [PDF]

				J.-C. Zeeh, M. Zeghouf, C. Grauffel, B. Guibert, E. Martin, A. Dejaegere, and J. Cherfils Dual Specificity of the Interfacial Inhibitor Brefeldin A for Arf Proteins and Sec7 Domains J. Biol. Chem., April 28, 2006; 281(17): 11805 - 11814. [Abstract] [Full Text] [PDF]

				M. T. Madziva and M. Birnbaumer A Role for ADP-ribosylation Factor 6 in the Processing of G-protein-coupled Receptors J. Biol. Chem., April 28, 2006; 281(17): 12178 - 12186. [Abstract] [Full Text] [PDF]

				P. F. Esteban, H.-Y. Yoon, J. Becker, S. G. Dorsey, P. Caprari, M. E. Palko, V. Coppola, H. U. Saragovi, P. A. Randazzo, and L. Tessarollo A kinase-deficient TrkC receptor isoform activates Arf6-Rac1 signaling through the scaffold protein tamalin J. Cell Biol., April 24, 2006; 173(2): 291 - 299. [Abstract] [Full Text] [PDF]

				W. Choi, Z. A. Karim, and S. W. Whiteheart Arf6 plays an early role in platelet activation by collagen and convulxin Blood, April 15, 2006; 107(8): 3145 - 3152. [Abstract] [Full Text] [PDF]

				S. Mukherjee, M. Tessema, and A. Wandinger-Ness Vesicular Trafficking of Tyrosine Kinase Receptors and Associated Proteins in the Regulation of Signaling and Vascular Function Circ. Res., March 31, 2006; 98(6): 743 - 756. [Abstract] [Full Text] [PDF]

				M. Z. Meyer, N. Deliot, S. Chasserot-Golaz, R. T. Premont, M.-F. Bader, and N. Vitale Regulation of Neuroendocrine Exocytosis by the ARF6 GTPase-activating Protein GIT1 J. Biol. Chem., March 24, 2006; 281(12): 7919 - 7926. [Abstract] [Full Text] [PDF]

				M. Li, S. S.-m. Ng, J. Wang, L. Lai, S. Yi Leung, M. Franco, Y. Peng, M.-l. He, H.-f. Kung, and M. C.-m. Lin EFA6A Enhances Glioma Cell Invasion through ADP Ribosylation Factor 6/Extracellular Signal-Regulated Kinase Signaling Cancer Res., February 1, 2006; 66(3): 1583 - 1590. [Abstract] [Full Text] [PDF]

				S. Krugmann, S. Andrews, L. Stephens, and P. T. Hawkins ARAP3 is essential for formation of lamellipodia after growth factor stimulation J. Cell Sci., February 1, 2006; 119(3): 425 - 432. [Abstract] [Full Text] [PDF]

				S. E. Robertson, S. R. G. Setty, A. Sitaram, M. S. Marks, R. E. Lewis, and M. M. Chou Extracellular Signal-regulated Kinase Regulates Clathrin-independent Endosomal Trafficking Mol. Biol. Cell, February 1, 2006; 17(2): 645 - 657. [Abstract] [Full Text] [PDF]

				J. R. Silvius, P. Bhagatji, R. Leventis, and D. Terrone K-ras4B and Prenylated Proteins Lacking "Second Signals" Associate Dynamically with Cellular Membranes Mol. Biol. Cell, January 1, 2006; 17(1): 192 - 202. [Abstract] [Full Text] [PDF]

				O. A. Jovanovic, F. D. Brown, and J. G. Donaldson An Effector Domain Mutant of Arf6 Implicates Phospholipase D in Endosomal Membrane Recycling Mol. Biol. Cell, January 1, 2006; 17(1): 327 - 335. [Abstract] [Full Text] [PDF]

				L. Liu, H. Liao, A. Castle, J. Zhang, J. Casanova, G. Szabo, and D. Castle SCAMP2 Interacts with Arf6 and Phospholipase D1 and Links Their Function to Exocytotic Fusion Pore Formation in PC12 Cells Mol. Biol. Cell, October 1, 2005; 16(10): 4463 - 4472. [Abstract] [Full Text] [PDF]

				N. Naslavsky and S. Caplan C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH? J. Cell Sci., September 15, 2005; 118(18): 4093 - 4101. [Abstract] [Full Text] [PDF]

				K.-S. Chae, K.-S. Oh, and S. E. Dryer Growth Factors Mobilize Multiple Pools of KCa Channels in Developing Parasympathetic Neurons: Role of ADP-Ribosylation Factors and Related Proteins J Neurophysiol, August 1, 2005; 94(2): 1597 - 1605. [Abstract] [Full Text] [PDF]

				Z. Nie, J. Fei, R. T. Premont, and P. A. Randazzo The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3 J. Cell Sci., August 1, 2005; 118(15): 3555 - 3566. [Abstract] [Full Text] [PDF]

				R. Galandrini, F. Micucci, I. Tassi, M. G. Cifone, B. Cinque, M. Piccoli, L. Frati, and A. Santoni Arf6: a new player in Fc{gamma}RIIIA lymphocyte-mediated cytotoxicity Blood, July 15, 2005; 106(2): 577 - 583. [Abstract] [Full Text] [PDF]

				K. Venkateswarlu, T. Hanada, and A. H. Chishti Centaurin-{alpha}1 interacts directly with kinesin motor protein KIF13B J. Cell Sci., June 1, 2005; 118(11): 2471 - 2484. [Abstract] [Full Text] [PDF]

				N. Touret, P. Paroutis, and S. Grinstein The nature of the phagosomal membrane: endoplasmic reticulum versus plasmalemma J. Leukoc. Biol., June 1, 2005; 77(6): 878 - 885. [Abstract] [Full Text] [PDF]

				J. Lawrence, S. J. Mundell, H. Yun, E. Kelly, and K. Venkateswarlu Centaurin-{alpha}1, an ADP-Ribosylation Factor 6 GTPase Activating Protein, Inhibits {beta}2-Adrenoceptor Internalization Mol. Pharmacol., June 1, 2005; 67(6): 1822 - 1828. [Abstract] [Full Text] [PDF]

				M. E. Balana, F. Niedergang, A. Subtil, A. Alcover, P. Chavrier, and A. Dautry-Varsat ARF6 GTPase controls bacterial invasion by actin remodelling J. Cell Sci., May 15, 2005; 118(10): 2201 - 2210. [Abstract] [Full Text] [PDF]

				K. Aoyagi, T. Sugaya, M. Umeda, S. Yamamoto, S. Terakawa, and M. Takahashi The Activation of Exocytotic Sites by the Formation of Phosphatidylinositol 4,5-Bisphosphate Microdomains at Syntaxin Clusters J. Biol. Chem., April 29, 2005; 280(17): 17346 - 17352. [Abstract] [Full Text] [PDF]

				A. Honda, O. S. Al-Awar, J. C. Hay, and J. G. Donaldson Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARE J. Cell Biol., March 28, 2005; 168(7): 1039 - 1051. [Abstract] [Full Text] [PDF]

				Y. Liu, G. M. Yerushalmi, P. R. Grigera, and J. T. Parsons Mislocalization or Reduced Expression of Arf GTPase-activating Protein ASAP1 Inhibits Cell Spreading and Migration by Influencing Arf1 GTPase Cycling J. Biol. Chem., March 11, 2005; 280(10): 8884 - 8892. [Abstract] [Full Text] [PDF]

				S. Ikeda, M. Ushio-Fukai, L. Zuo, T. Tojo, S. Dikalov, N. A. Patrushev, and R. W. Alexander Novel Role of ARF6 in Vascular Endothelial Growth Factor-Induced Signaling and Angiogenesis Circ. Res., March 4, 2005; 96(4): 467 - 475. [Abstract] [Full Text] [PDF]

				K. J. Roux, S. A. Amici, B. S. Fletcher, and L. Notterpek Modulation of Epithelial Morphology, Monolayer Permeability, and Cell Migration by Growth Arrest Specific 3/Peripheral Myelin Protein 22 Mol. Biol. Cell, March 1, 2005; 16(3): 1142 - 1151. [Abstract] [Full Text] [PDF]

				K.-F. Xu, X. Shen, H. Li, G. Pacheco-Rodriguez, J. Moss, and M. Vaughan Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70 PNAS, February 22, 2005; 102(8): 2784 - 2789. [Abstract] [Full Text] [PDF]

				Q. Lu, W. Wei, P. E. Kowalski, A. C. Y. Chang, and S. N. Cohen EST-based genome-wide gene inactivation identifies ARAP3 as a host protein affecting cellular susceptibility to anthrax toxin PNAS, December 7, 2004; 101(49): 17246 - 17251. [Abstract] [Full Text] [PDF]

				H.-W. Shin and K. Nakayama Guanine Nucleotide-Exchange Factors for Arf GTPases: Their Diverse Functions in Membrane Traffic J. Biochem., December 1, 2004; 136(6): 761 - 767. [Abstract] [Full Text] [PDF]

				L. Hertel and E. S. Mocarski Global Analysis of Host Cell Gene Expression Late during Cytomegalovirus Infection Reveals Extensive Dysregulation of Cell Cycle Gene Expression and Induction of Pseudomitosis Independent of US28 Function J. Virol., November 1, 2004; 78(21): 11988 - 12011. [Abstract] [Full Text] [PDF]

				A. Ono, S. D. Ablan, S. J. Lockett, K. Nagashima, and E. O. Freed Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane PNAS, October 12, 2004; 101(41): 14889 - 14894. [Abstract] [Full Text] [PDF]

				B. A. Jordan, B. D. Fernholz, M. Boussac, C. Xu, G. Grigorean, E. B. Ziff, and T. A. Neubert Identification and Verification of Novel Rodent Postsynaptic Density Proteins Mol. Cell. Proteomics, September 1, 2004; 3(9): 857 - 871. [Abstract] [Full Text] [PDF]

				C. A. Smith, S. E. Dho, J. Donaldson, U. Tepass, and C. J. McGlade The Cell Fate Determinant Numb Interacts with EHD/Rme-1 Family Proteins and Has a Role in Endocytic Recycling Mol. Biol. Cell, August 1, 2004; 15(8): 3698 - 3708. [Abstract] [Full Text] [PDF]

				M. R. Wenk and P. De Camilli Inaugural Article: Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: Insights from vesicle recycling in nerve terminals PNAS, June 1, 2004; 101(22): 8262 - 8269. [Abstract] [Full Text] [PDF]

				S. Hashimoto, Y. Onodera, A. Hashimoto, M. Tanaka, M. Hamaguchi, A. Yamada, and H. Sabe Requirement for Arf6 in breast cancer invasive activities PNAS, April 27, 2004; 101(17): 6647 - 6652. [Abstract] [Full Text] [PDF]

				R. Cox, R. J Mason-Gamer, C. L. Jackson, and N. Segev Phylogenetic Analysis of Sec7-Domain-containing Arf Nucleotide Exchangers Mol. Biol. Cell, April 1, 2004; 15(4): 1487 - 1505. [Abstract] [Full Text] [PDF]

				P. I. Padilla, G. Pacheco-Rodriguez, J. Moss, and M. Vaughan Nuclear localization and molecular partners of BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors PNAS, March 2, 2004; 101(9): 2752 - 2757. [Abstract] [Full Text] [PDF]

				K. Venkateswarlu, K. G. Brandom, and J. L. Lawrence Centaurin-{alpha}1 Is an in Vivo Phosphatidylinositol 3,4,5-Trisphosphate-dependent GTPase-activating Protein for ARF6 That Is Involved in Actin Cytoskeleton Organization J. Biol. Chem., February 20, 2004; 279(8): 6205 - 6208. [Abstract] [Full Text] [PDF]

This Article Full Text (PDF) All Versions of this Article: 278/43/41573    most recent R300026200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Donaldson, J. G. Search for Related Content PubMed PubMed Citation Articles by Donaldson, J. G. Social Bookmarking                      What's this?