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Article

Src-Dependent Phosphorylation of ASAP1 Regulates Podosomes

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Pages 8271-8283 | Received 20 Sep 2006, Accepted 14 Sep 2007, Published online: 27 Mar 2023

REFERENCES

  • Arold, S., P. Franken, M. P. Strub, F. Hoh, S. Benichou, R. Benarous, and C. Dumas. 1997. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. Structure 5:1361–1372.
  • Bowden, E. T., M. Barth, D. Thomas, R. I. Glazer, and S. C. Mueller. 1999. An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18:4440–4449.
  • Brown, M. T., J. Andrade, H. Radhakrishna, J. G. Donaldson, J. A. Cooper, and P. A. Randazzo. 1998. ASAP1, a phospholipid-dependent Arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell. Biol. 18:7038–7051.
  • Brunton, V. G., I. R. J. MacPherson, and M. C. Frame. 2004. Cell adhesion receptors, tyrosine kinases and actin modulators: a complex three-way circuitry. Biochim. Biophys. Acta 1692:121–144.
  • Buccione, R., J. D. Orth, and M. A. McNiven. 2004. Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nat. Rev. Mol. Cell Biol. 5:647–657.
  • Carragher, N. O., and M. C. Frame. 2004. Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion. Trends Cell Biol. 14:241–249.
  • Ehlers, J. P., L. Worley, M. D. Onken, and J. W. Harbour. 2005. DDEF1 is located in an amplified region of chromosome 8q and is overexpressed in uveal melanoma. Clin. Cancer Res. 11:3609–3613.
  • Farsad, K., and P. De Camilli. 2003. Mechanisms of membrane deformation. Curr. Opin. Cell Biol. 15:372–381.
  • Farsad, K., N. Ringstad, K. Takei, S. R. Floyd, K. Rose, and P. De Camilli. 2001. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J. Cell Biol. 155:193–200.
  • Furman, C., S. M. Short, R. R. Subramanian, B. R. Zetter, and T. M. Roberts. 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.
  • Gimona, M., and R. Buccione. 2006. Adhesions that mediate invasion. Int. J. Biochem. Cell Biol. 38:1875–1892.
  • Hashimoto, S., M. Hirose, A. Hashimoto, M. Morishige, A. Yamada, H. Hosaka, K. I. Akagi, E. Ogawa, C. Oneyama, T. Agatsuma, M. Okada, H. Kobayashi, H. Wada, H. Nakano, T. Ikegami, A. Nakagawa, and H. Sabe. 2006. Targeting AMAP1 and cortactin binding bearing an atypical Src homology 3/proline interface for prevention of breast cancer invasion and metastasis. Proc. Natl. Acad. Sci. USA 103:7036–7041.
  • Hayasaka, H., K. Simon, E. D. Hershey, K. Masumoto, and J. T. Parsons. 2005. FRNK, the autonomously expressed C-terminal region of focal adhesion kinase, is uniquely regulated in vascular smooth muscle: analysis of expression in transgenic mice. J. Cell. Biochem. 95:1248–1263.
  • Itoh, T., and P. De Camilli. 2006. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochim. Biophys. Acta 1761:897–912.
  • Juliano, R. L. 2002. Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu. Rev. Pharmacol. Toxicol. 42:283–323.
  • King, F. J., E. D. Hu, D. F. Harris, P. Sarraf, B. M. Spiegelman, and T. M. Roberts. 1999. DEF-1, a novel Src SH3 binding protein that promotes adipogenesis in fibroblastic cell lines. Mol. Cell. Biol. 19:2330–2337.
  • Kowanetz, K., K. Husnjak, D. Holler, M. Kowanetz, P. Soubeyran, D. Hirsch, M. H. H. Schmidt, K. Pavelic, P. De Camilli, P. A. Randazzo, and I. Dikic. 2004. CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors. Mol. Biol. Cell 15:3155–3166.
  • Kruljac-Letunic, A., J. Moelleken, A. Kallin, F. Wieland, and A. Blaukat. 2003. The tyrosine kinase Pyk2 regulates Arf1 activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAP1. J. Biol. Chem. 278:29560–29570.
  • Lee, C. H., B. Leung, M. A. Lemmon, J. Zheng, D. Cowburn, J. Kuriyan, and K. Saksela. 1995. A single amino-acid in the SH3 domain of Hck determines its high-affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14:5006–5015.
  • Lee, C. H., K. Saksela, U. A. Mirza, B. T. Chait, and J. Kuriyan. 1996. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85:931–942.
  • Liu, Y., J. C. Loijens, K. H. Martin, A. V. Karginov, and J. T. Parsons. 2002. The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly. Mol. Biol. Cell 13:2147–2156.
  • Liu, Y., G. M. Yerushalmi, P. R. Grigera, and J. T. Parsons. 2005. Mislocalization or reduced expression of Arf GTPase-activating protein ASAP1 inhibits cell spreading and migration by influencing Arf1 GTPase cycling. J. Biol. Chem. 280:8884–8892.
  • Luo, R., B. Ahvazi, D. Amariei, D. Shroder, B. Burrola, W. Losert, and P. A. Randazzo. 2007. Kinetic analysis of GTP hydrolysis catalysed by the Arf1-GTP-ASAP1 complex. Biochem. J. 402:439–447.
  • Mclean, G. W., N. O. Carragher, E. Avizienyte, J. Evans, V. G. Brunton, and M. C. Frame. 2005. The role of focal-adhesion kinase in cancer—a new therapeutic opportunity. Nat. Rev. Cancer 5:505–515.
  • Nam, J. M., Y. Onodera, Y. Mazaki, H. Miyoshi, S. Hashimoto, and H. Sabe. 2007. CIN85, a Cbl-interacting protein, is a component of AMAP1-mediated breast cancer invasion machinery. EMBO J. 26:647–656.
  • Nie, Z., M. Boehm, E. Boja, W. Vass, J. Bonifacino, H. Fales, and P. A. Randazzo. 2003. Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1. Dev. Cell 5:513–521.
  • Nie, Z., D. S. Hirsch, R. Luo, X. Jian, S. Stauffer, A. Cremesti, J. Andrade, J. Lebowitz, M. Marino, B. Ahvazi, J. E. Hinshaw, and P. A. Randazzo. 2006. A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor. Curr. Biol. 16:130–139.
  • Oda, A., I. Wada, K. Miura, K. Okawa, T. Kadoya, T. Kato, H. Nishihara, M. Maeda, S. Tanaka, K. Nagashima, C. Nishitani, K. Matsuno, M. Ishino, L. M. Machesky, H. Fujita, and P. Randazzo. 2003. CrkL directs ASAP1 to peripheral focal adhesions. J. Biol. Chem. 278:6456–6460.
  • Onodera, Y., S. Hashimoto, A. Hashimoto, M. Morishige, A. Yamada, E. Ogawa, M. Adachi, T. Sakurai, T. Manabe, H. Wada, N. Matsuura, and H. Sabe. 2005. Expression of AMAP1, an ArfGAP, provides novel targets to inhibit breast cancer invasive activities. EMBO J. 24:963–973.
  • Parsons, J. T. 2003. Focal adhesion kinase: the first ten years. J. Cell Sci. 116:1409–1416.
  • Parsons, J. T., K. H. Martin, J. K. Slack, J. M. Taylor, and S. A. Weed. 2000. Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene 19:5606–5613.
  • Peter, B. J., H. M. Kent, I. G. Mills, Y. Vallis, P. J. G. Butler, P. R. Evans, and H. T. McMahon. 2004. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303:495–499.
  • Randazzo, P. A., J. Andrade, K. Miura, M. T. Brown, Y. Q. Long, S. Stauffer, P. Roller, and J. A. Cooper. 2000. The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton. Proc. Natl. Acad. Sci. USA 97:4011–4016.
  • Randazzo, P. A., and D. S. Hirsch. 2004. Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell. Signal. 16:401–413.
  • Turner, C. E., M. D. Schaller, and J. T. Parsons. 1993. Tyrosine phosphorylation of the focal adhesion kinase pp125FAK during development relation to paxillin. J. Cell Sci. 105:637–645.
  • Webb, D. J., J. T. Parsons, and A. F. Horwitz. 2002. Adhesion assembly, disassembly and turnover in migrating cells—over and over and over again. Nat. Cell Biol. 4:E97–E100.
  • Wehrle-Haller, B., and B. A. Imhof. 2002. The inner lives of focal adhesions. Trends Cell Biol. 12:382–389.

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