Abstract
Cell migration is a multifactorial process in which a number of distinct events occur simultaneously. Paxillin is an integrin-assembly adaptor protein. Here, properties of Arf GAPs bearing paxillin-binding capacity are described with their isoform specificity. Roles in linking Arf function with other intracellular events all need to be coordinately regulated during integrin-mediated cell adhesion and migration.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Aderem, A., and Underhill, D. M. (1999). Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol., 17, 593–623.
Aggeler, J., and Werb, Z. (1982). Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin. J. Cell Biol., 94, 613–623.
Al-Awar, O., Radhakrishna, H., Powell, N. N., and Donaldson, J. G. (2000). Separation of membrane trafficking and actin remodeling functions of ARF6 with an effector domain mutant. Mol. Cell. Biol., 20, 5998–6007.
Allen, L. H., and Aderem, A. (1996). Molecular definition of distinct cytoskeletal structures involved in complement-and Fc receptor-mediated phagocytosis in macrophages. J. Exp. Med., 184, 627–637.
Andreev, J., Simon, J., Sabatini, D. D., Kam, J., Plowman, G., Randazzo, P.A., and Schlessinger, J. (1999). Identification of a new Pyk2 target protein with Arf-GAP activity. Mol. Cell. Biol., 19, 2338–2350.
Bajno, L., Peng, X. R., Schreiber, A. D., Moore, H. P., Trimble, W. S., and Grinstein, S. (2000). Focal exocytosis of VAMP3-containing vesicles at sites of phagosome formation. J. Cell Biol., 149, 697–706.
Bagrodia, S., Taylor, S. J., Jordon, K. A., Van Aelst, L., and Cerione, R. A. (1998). A novel regulator of p21-activated kinases. J. Biol. Chem., 273, 23633–23636.
Bagrodia, S., Bailey, D., Lenard, Z., Hart, M., Guan, J. L., Premont, R. T., Taylor, S. J., and Cerione, R. A. (1999). A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins. J. Biol. Chem., 274, 22393–22400.
Bagrodia, S., and Cerione, R. A. (1999). Pak to the future. Trends Cell Biol., 9, 350–355.
Bockoch, G. M., Wang, Y., Bohl, B. P., Sells, M. A., Quilliam, L. A., and Knaus, U. G. (1996). Interaction of the Nck adapter protein with p21-activated kinase (PAK1). J. Biol. Chem., 271, 25746–25749.
Borisy, G. G., and Svitkina, T. M. (2000). Actin machinery: pushing the envelope. Curr. Opin. Cell Biol., 12, 104–112.
Boshans, R. L., Szanto, S., van Aelst, L., and D’Souza-Schorey, C. (2000). ADP-ribosylation factor 6 regulates actin cytoskeleton remodeling in coordination with Rac1 and RhoA. Mol. Cell Biol., 20, 3685–3694
Bretscher, M. S. (1996). Getting membrane flow and the cytoskeleton to cooperate in moving cells. Cell, 87, 601–606.
Bretscher, M. S. (1989). Endocytosis and recycling of the fibronectin receptor in CHO cells. EMBO J., 8, 1341–1348.
Bretscher, M. S. (1992). Circulating integrins: α5β1, α6β4 and Mac-1, but not α3β1, α4β1 or LFA-1. EMBO J., 11, 405–410.
Brown, M. T., Andrade, J., Radhakrishna, H., Donaldson, J. G., Cooper, J. A., and Randazzo, P. A. (1998). ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell Biol., 18, 7038–7051.
Brown, F. D., Rozelle, A. L., Yin, H. L., Bella, T., and Donaldson, J. G. (2001). Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol., 154, 1007–1017.
Brown, M. C., West, K. A., and Turner, C. E. (2002). Paxillin-dependent Paxillin Kinase Linker and p21-Activated Kinase Localization to Focal Adhesions Involves a Multistep Activation Pathway. Mol. Biol. Cell, 13, 1550–1565.
Cavenagh, M. M., Whitney, J. A., Carrol, K., Zhang, C.-J., Boman, A. L., Rosenwald, A.G., Mellman, I., and Kahn, R. A. (1996). Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane. J. Biol. Chem., 271, 21767–21774.
Chardin, P., and McCormick, F. (1999). Brefeldin A: the advantage of being uncompetitive. Cell, 97, 153–155.
Corbett, K. D., and Alber, T. (2001). The many faces of Ras: recognition of small GTP-binding proteins. Trends Biochem. Sci., 26, 710–716.
Cox, D., Tseng, C. C., Bjekic, G., and Greenberg, S. (1999). A requirement for phosphatidylinositol 3-kinase in pseudopod extension. J. Biol. Chem., 274, 1240–1247.
Cukierman, E., Huber, I., Rotman, M., and Cassel. D. (1995). The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science, 270, 1999–2002.
Daniels, R. H., Zenke, F. T. and Bokoch, G. M. (1999). αPix stimulates p21-activated kinase activity through exchange factor-dependent and-independent mechanisms. J. Biol. Chem., 274, 6047–6050.
de Curtis, I. (2001) Cell migration: GAPs between membrane traffic and the cytoskeleton. EMBO R., 2, 277–281.
Del Pozo, M. A., Kiosses, W. B., Alderson, N. B., Meller, N., Hahn, K. M., and Schwartz, M. A. (2002). Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI. Nature Cell Biol., 4, 232–239.
Di Cesare, A., Paris, S., Albertinazzi, C., Dariozzi, S., Andersen, J., Mann, M., Longhi, R., and de Curtis, I. (2000). p95-APP1 links membrane transport to Rac-mediated reorganization of actin. Nat. Cell Biol., 2, 521–530.
D’Souza-Schorey, C., Li, G., Colombo, M. I, and Stahl, P. D. (1995). A reglatory role for ARF6 in receptor-mediated endocytosis. Science, 267, 1175–1178.
D’Souza-Schorey, C., van Donselaar, E., Hsu, V. W., Yang, C., Stahl, P. D., and Peters, P. J. (1998). ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation. J. Cell Biol., 140, 603–616.
Erickson, J. W., Zhang, C., Kahn, R. A., Evans, T., and Cerione, R. A. (1996). Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem., 271, 26850–26854.
Eugster, A., Frigerio, G., Dale, M., and Duden, R. (2000). COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP. EMBO J., 19, 3905–3917.
Furman, C., Short, S. M., Subramanian, R. R., Zetter, B. R., and Roberts, T. M. (2002). DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that enhances cell motility through a GAP-dependent mechanism. J. Biol. Chem., 277, 7962–7969.
Galisteo, M. L., Chernoff, J., Su, Y.C., Skolnik, E. Y., and Schlessinger, J. (1996). The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem., 271, 20997–21000.
Goldberg, J. (1999). Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell, 96, 893–902.
Greenberg, S., Chang, P., and Silverstein, S. C. (1994). Tyrosine phosphorylation of the γ subunit of Fcγ receptors, p72syk, and paxillin during Fc receptor-mediated phagocytosis in macrophages. J. Biol. Chem., 269, 3897–3902.
Greenberg, S. (1999). Molecular components of phagocytosis. J. Leukoc. Biol., 66, 712–717.
Hart, M. J., Eva, A., Zangrilli, D., Aaronson, S. A., Evans, T., Cerione, R. A., and Zheng, Y. (1994). Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem., 269, 62–65.
Hashimoto, S., Tsubouchi, A., Mazaki, Y., and Sabe, H. (2001). Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin a with the kinase-inactive and the Cdc42-activated forms of PAK3. J. Biol. Chem., 278, 6037–6045.
Hussain, N. K., Jenna, S., Glogauer, M., Quinn, C. C., Wasiak, S., Guipponi, M., Antonarakis, S. E., Kay, B. K., Stossel, T. P., Lamarche-Vane, N., and McPherson, P. S. (2001). Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP. Nat. Cell Biol., 3, 927–932.
Hynes, R. O. (2002). Integrins: bidirectional, allosteric signaling machines. Cell, 110, 673–687.
Kahn, R. A., and Gilman, A. G. (1986). The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem., 261, 7906–7911.
King, F. J., Hu, E., Harris, D.F., Sarraf, P., Spiegelman, B. M., and Roberts, T. M. (1999). DEF-1, a novel Src SH3 binding protein that promotes adipogenesis in fibroblastic cell lines. Mol. Cell. Biol., 19, 2330–2337.
Kondo, A., Hashimoto, S., Yano, H., Nagayama, K., Mazaki, Y., and Sabe, H. (2000). A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration. Mol. Biol. Cell, 11, 1315–1327.
Kraynov, V. S., Chamberlain, C., Bokoch, G. M., Schwartz, M. A., Slabaugh, S., and Hahn, K. M. (2000). Localized Rac activation dynamics visualized in living cells. Science, 290, 333–337.
Kroschewski, R., Hall, A., and Mellman, I. (1999). Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nature Cell Biol., 1, 8–13.
Lawson, M. A., and Maxfield, F. R. (1995). Ca(2+)-and calcineurin-dependent recycling of an integrin to the front of migrating neutrophils. Nature, 377, 75–79.
Laukaitis, C. M., Webb, D. J., Donais, K., and Horwitz, A. F. (2001). Differential dynamics of a5 integrin, paxillin, and a-actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol., 153, 1427–1440.
Lu, W., Katz, S., Gupta, R., and Mayer, B. J. (1997). Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol., 7, 85–94.
Manabe, R., Kovalenko, M., Webb, D. J., and Horwitz, A. R. (2002). GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J. Cell Sci., 115, 1497–1510.
Mandiyan, V., Andreev, J., Schlessinger, J., and Hubbard, S. R. (1999). Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta. EMBO J., 18, 6890–6898.
Manser, E., Leung, T., Salihuddin, H., Zhao, Z. S., and Lim, L. (1994). A brain serine/ threonine ptotein kinase activated by Cdc42 and Rac1. Nature, 367, 40–46.
Manser, E., Loo, T. H., Koh, C. G., Zhao, Z. S., Chen, X. Q., Tan, L., Tan, I., Leung, T., and Lim, L. (1998). PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Mol. Cell, 1, 183–192.
Mazaki, Y., Hashimoto, S., and Sabe, H. (1997). Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins. J. Biol. Chem., 272, 7437–7444.
Mazaki, Y., Uchida, H., Hino, O., Hashimoto, S., and Sabe, H. (1998). Paxillin isoforms in mouse. Lack of the γ isoform and developmentally specific beta isoform expression. J. Biol. Chem., 273, 22435–22441.
Mazaki, Y., Hashimoto, S., Okawa, K., Nakamura, K., Yagi, R., Yano, H., Kondo, A., Iwamatsu, A., Mizoguchi, A., and Sabe, H. (2001). An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization. Mol. Biol. Cell. 12, 645–662.
Mitchison, T. J., and Cramer, L. P. (1996). Actin-Based Cell Motility and Cell Locomotion. Cell, 84, 371–379.
Miyamoto, S., Akiyama, S. K., and Yamada, K. M. (1995a). Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science, 267, 883–885.
Miyamoto, S., Teramoto, H., Coso, O. A., Gutkind, J. S., Burbelo, P. D., Akiyama, S. K., and Yamada, K. M. (1995b). Integrin function: molecular hierarchies of cytoskeletal and signaling molecules. J. Cell Biol., 131, 791–805.
Nakamura, K., Yano, H., Uchida, H., Hashimoto, S., and Sabe, H. (2000). Tyrosine phosphorylation of paxillin a is involved in temporospatial regulation of paxillin-containing focal adhesion formation and F-actin organization in motile cells. J. Biol. Chem., 275, 27155–27164.
Nakashima, S., Morinaka, K., Koyama, S., Ikeda, M., Kishida, M., Okawa, K., Iwamatsu, A., Kishida, S., and Kikuchi, A. (1999). Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors. EMBO J., 18, 3629–4362.
Norman, J. C., Jones, D., Barry, S. T., Holt, M. R., Cockcroft, S., and Critchley, D.R. (1998). ARF1 mediates paxillin recruitment to focal adhesions and potentiates Rho-stimulated stress fiber formation in intact and permeabilized Swiss 3T3 fibroblasts. J. Cell Biol., 143, 1981–1995.
Ooi, C. E., DelľAngelica, E. C., and Bonifacino, J. S. (1998). ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol., 142, 391–402.
Oshiro, T., Koyama, S., Sugiyama, S., Kondo, A., Onodera, Y., Asahara, T., Sabe, H., and Kikuchi A. (2002). Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin binding protein, is involved in cell migration. J. Biol. Chem., 277, 38618–38626.
Peters, P. J., Hsu, V. W., Ooi, C. E., Finazzi, D., Teal, S. B., Oorschot, V., Donaldson, J. G., and Klausner, R. D. (1995). Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J. Cell Biol., 128, 1003–1017.
Premont, R. T., Claing, A., Vitale, N., Freeman, J. L., Pitcher, J. A., Patton, W. A., Moss, J., Vaughan, M., and Lefkowitz, R. J. (1998). β2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein. Proc. Natl. Acad. Sci., USA, 95, 14082–14087.
Premont, R. T., Claing, A., Vitale, N., Perry, S. J., and Lefkowitz, R. J. (2000). The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing. J. Biol. Chem., 275, 22373–22380.
Radhakrishna, H., Klausner, R. D., and Donaldson, J. G. (1996). Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol., 134, 935–947.
Radhakrishna, H., and Donaldson, J. G. (1997). ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway. J. Cell Biol., 139, 49–61.
Regen, C. M., and Horwitz A. F. (1992). Dynamics of β1 integrin-mediated adhesive contacts in motile fibroblasts. J Cell Biol., 119, 1347–1359.
Ridley, A. J., Self, A. J., Kasmi, F., Paterson, H. F., Hall, A., Marshall, C. J., and Ellis, C. (1993). rho family GTPase activating proteins p190, bcr and rhoGAP show distinct specificities in vitro and in vivo. EMBO J., 12, 5151–5160.
Ridley, A. J. (2001). Rho proteins: linking signaling with membrane trafficking. Traffic, 2, 303–310.
Roberts, M., Barry, S., Woods, A., van der Sluijs, P., and Norman, J. (2001). PDGF-regulated rab4-dependent recycling of avβ3 integrin from early endosomes is necessary for cell adhesion and spreading. Curr. Biol., 11, 1392–1402.
Roth, M. G. (1999). Snapshots of ARF1: Implications for Mechanisms of Activation and Inactivation. Cell, 97, 149–152.
Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science, 271, 1526–1533.
Scheffzek, K., Ahmadian, M. R., Wiesmuller, L., Kabsch, W., Stege, P., Schmitz, F., and Wittinghofer, A. (1998). Structural analysis of the GAP-related domain from neurofibromin and its implications. EMBO J., 17, 4313–4327.
Settleman, J., Albright, C. F., Foster, L. C., and Weinberg, R. A. (1992). Association between GTPase activators for Rho and Ras families. Nature, 359, 153–155.
Springer, S., Spang, A., and Schekman, R. (1999). A primer on vesicle budding. Cell, 97, 145–148.
Sternweis, P. C., and Gilman, A. G. (1982). Aluminum: a requirement for activation of the regulatory component of adenylate cyclase by fluoride. Proc. Natl. Acad. Sci., USA, 79, 4888–4891.
Stowers, L., Yelon, D., Berg, L. J., and Chant, J. (1995) Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc. Natl. Acad. Sci., USA, 92, 5027–5031.
Szafer, E., Pick, E., Rotman, M., Zuck, S., Huber, I., and Cassel, D. (2000). Role of coatomer and phospholipids in GTPase-activating protein-dependent hydrolysis of GTP by ADP-ribosylation factor-1. J. Biol. Chem., 275, 23615–23619.
Tsubouchi, A., Sakakura, J., Yagi, R., Mazaki, Y., Schaefer, E., Yano, H., and Sabe, H. (2002). Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion nd migration. J. Cell Biol., 159, 673–683.
Turner, C. E., Brown, M. C., Perrotta, J. A., Riedy, M. C., Nikolopoulos, S. N., McDonald, A. R., Bagrodia, S., Thomas, S., and Leventhal, P. S. (1999). Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. J. Cell Biol., 145, 851–863.
Turner, C. E. (2000). Paxillin and focal adhesion signalling. Nature Cell Biol., 2, E231–E236.
Uchida, H., Kondo, A., Yoshimura, Y., Mazaki, Y., and Sabe, H. (2001). PAG3/Papa/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcγ receptor-mediated phagocytosis of macrophages. J. Exp. Med., 193, 955–966.
Vitale, N., Patton, W. A., Moss, J., Vaughan, M., Lefkowitz, R. J., and Premont, R. T. (2000). GIT proteins, A novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6. J. Biol. Chem., 275, 13901–13906.
Wu, W. J., Erickson, J. W., Lin, R., and Cerione, R. A. (2000). The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature, 405, 800–804.
Zhang, Q., Cox, D., Tseng, C.C., Donaldson, J.G., and Greenberg, S.(1998). A requirement for ARF6 in Fcγ receptor-mediated phagocytosis in macrophages. J. Biol. Chem., 273, 19977–19981.
Zhao, Z. S., Manser, E., Loo, T. H., and Lim, L. (2000). Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol., 20, 6354–6363.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2004 Springer Science + Business Media, Inc.
About this chapter
Cite this chapter
Sabe, H. (2004). Paxillin-Associated Arf GAPs. In: ARF Family GTPases. Proteins and Cell Regulation, vol 1. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2593-9_9
Download citation
DOI: https://doi.org/10.1007/1-4020-2593-9_9
Publisher Name: Springer, Dordrecht
Print ISBN: 978-1-4020-1719-3
Online ISBN: 978-1-4020-2593-8
eBook Packages: Springer Book Archive