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Volumn 14, Issue 3, 2003, Pages 1085-1096

A dynamin-cortactin-Arp2/3 complex mediates actin reorganization in growth factor-stimulated cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; CORTACTIN; DYNAMIN; GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR;

EID: 0037343053     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-08-0466     Document Type: Article
Times cited : (186)

References (42)
  • 2
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCm associates with invadopodia at sites of extracellular matrix degradation
    • Bowden, E.T., Barth, M., Thomas, D., Glazer, R.I., and Mueller, S.C. (1999). An invasion-related complex of cortactin, paxillin and PKCm associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18, 4440-4449.
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 3
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • Cao, H., Garcia, F., and McNiven, M. (1998). Differential distribution of dynamin isoforms in mammalian cells. Mol. Biol. Cell 9, 2595-2609.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.3
  • 4
    • 0032899885 scopus 로고    scopus 로고
    • Cytoskeletal and adhesive structural polarizations accompany IL- 13-induced human macrophage fusion
    • DeFife, K.M., Jenney, C.R., Colton, E., and Anderson, J.M. (1999). Cytoskeletal and adhesive structural polarizations accompany IL- 13-induced human macrophage fusion. J. Histol. Cytol. 47, 65-74.
    • (1999) J. Histol. Cytol. , vol.47 , pp. 65-74
    • DeFife, K.M.1    Jenney, C.R.2    Colton, E.3    Anderson, J.M.4
  • 5
    • 0032547385 scopus 로고    scopus 로고
    • Signal transduction via platelet-derived growth factor receptors
    • Heldin, C.H., Ostman, A., and Ronnstrand, L. (1998). Signal transduction via platelet-derived growth factor receptors. Biochem. Biophys. Acta 1378, F79-F113.
    • (1998) Biochem. Biophys. Acta , vol.1378
    • Heldin, C.H.1    Ostman, A.2    Ronnstrand, L.3
  • 7
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw, J.E. (2000). Dynamin and its role in membrane fission. Annu. Rev. Cell Dev. Biol. 16, 483-519.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 8
    • 0030971098 scopus 로고    scopus 로고
    • Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation
    • Huang, C., Yansong, N., Wang, T., Gao, Y., Haudenschild, C.C., and Zhan, X. (1997). Down-regulation of the filamentous actin cross-linking activity of cortactin by Src-mediated tyrosine phosphorylation. J. Biol. Chem. 272, 13911-13915.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13911-13915
    • Huang, C.1    Yansong, N.2    Wang, T.3    Gao, Y.4    Haudenschild, C.C.5    Zhan, X.6
  • 10
    • 0032566652 scopus 로고    scopus 로고
    • Expression of a dominant interfering dynamin mutant in 3T3L1 adipocytes inhibits GLUT4 endocytosis without affecting insulin signaling
    • Kao, A.W., Ceresa, B.P., Santeler, S.R., and Pessin, J.E. (1998). Expression of a dominant interfering dynamin mutant in 3T3L1 adipocytes inhibits GLUT4 endocytosis without affecting insulin signaling. J. Biol. Chem. 273, 25450-25457.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25450-25457
    • Kao, A.W.1    Ceresa, B.P.2    Santeler, S.R.3    Pessin, J.E.4
  • 12
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • Linder, S., Nelson, D., Weiss, M., and Aepfelbacher, M. (1999). Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages. Proc. Natl. Acad. Sci. USA 96, 9648-9653.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9648-9653
    • Linder, S.1    Nelson, D.2    Weiss, M.3    Aepfelbacher, M.4
  • 13
    • 0034161330 scopus 로고    scopus 로고
    • Pinching in new places: Multiple functions for the dynamin family
    • McNiven, M.A., Cao, H., Pitts, K.R., and Yoon, Y. (2000a). Pinching in new places: multiple functions for the dynamin family. Trends Biochem. Sci. 25, 115-120.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 115-120
    • McNiven, M.A.1    Cao, H.2    Pitts, K.R.3    Yoon, Y.4
  • 14
    • 0034597062 scopus 로고    scopus 로고
    • Interactions between dynamin and the actin binding protein cortactin modulate cell shape
    • McNiven, M.A., Kim, L., Krueger, E.W., Orth, J.D., Cao, H., and Wong, T.W. (2000b). Interactions between dynamin and the actin binding protein cortactin modulate cell shape. J. Cell Biol. 151, 187-198.
    • (2000) J. Cell Biol. , vol.151 , pp. 187-198
    • McNiven, M.A.1    Kim, L.2    Krueger, E.W.3    Orth, J.D.4    Cao, H.5    Wong, T.W.6
  • 15
    • 0023784627 scopus 로고
    • Induction of circular membrane ruffling on human fibroblasts by platelet-derived growth factor
    • Mellstrom, K., Heldin, C.H., and Westermark, B. (1988). Induction of circular membrane ruffling on human fibroblasts by platelet-derived growth factor. Exp. Cell Res. 177, 347-359.
    • (1988) Exp. Cell Res. , vol.177 , pp. 347-359
    • Mellstrom, K.1    Heldin, C.H.2    Westermark, B.3
  • 17
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., Miura, K., and Takenawa, T. (1996). N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326-5335.
    • (1996) EMBO J. , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 18
    • 0033960791 scopus 로고    scopus 로고
    • How WASP-family proteins, and the Arp2/3 complex convert intracellular signals into cytoskeletal structures
    • Mullins, R.D. (2000). How WASP-family proteins, and the Arp2/3 complex convert intracellular signals into cytoskeletal structures. Curr. Opin. Cell Biol. 12, 91-96.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 91-96
    • Mullins, R.D.1
  • 19
    • 0024341210 scopus 로고
    • The podosomes of Rous sarcoma virus transformed chondrocytes show a peculiar ultrastructural organization
    • Nitsch, L., Gionti, E., Cancedda, R., and Marchisio, P.C. (1989). The podosomes of Rous sarcoma virus transformed chondrocytes show a peculiar ultrastructural organization. Cell Biol. Int. Rep. 13, 919-926.
    • (1989) Cell Biol. Int. Rep. , vol.13 , pp. 919-926
    • Nitsch, L.1    Gionti, E.2    Cancedda, R.3    Marchisio, P.C.4
  • 20
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D., and Hall, A. (1995). Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 22
    • 0035921432 scopus 로고    scopus 로고
    • Abp1p and cortactin, new "hand-holds" for actin
    • Olazabal, I.M., and Machesky, L.M. (2001). Abp1p and cortactin, new "hand-holds" for actin. J. Cell Biol. 154, 679-682.
    • (2001) J. Cell Biol. , vol.154 , pp. 679-682
    • Olazabal, I.M.1    Machesky, L.M.2
  • 23
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth, J.D., Krueger, E.W., Cao, H., and McNiven, M.A. (2002). The large GTPase dynamin regulates actin comet formation and movement in living cells. Proc. Natl. Acad. Sci. USA 99, 167-172.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 24
    • 0030898418 scopus 로고    scopus 로고
    • Src family protein tyrosine kinases: Cooperating with growth factor and adhesion signaling pathways
    • Parsons, J.T., and Parsons, S.J. (1997). Src family protein tyrosine kinases: cooperating with growth factor and adhesion signaling pathways. Curr. Opin. Cell Biol. 9, 187-192.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 187-192
    • Parsons, J.T.1    Parsons, S.J.2
  • 26
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and stress fibers in response to growth factors
    • Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and stress fibers in response to growth factors. Cell. 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 27
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Peterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Peterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 28
    • 0031744448 scopus 로고    scopus 로고
    • Actin-dependent anterograde movement of growth-cone-like structures along growing hippocampal axons: A novel form of axonal transport?
    • Ruthel, G., and Banker, G. (1998). Actin-dependent anterograde movement of growth-cone-like structures along growing hippocampal axons: a novel form of axonal transport? Cell Motil. Cytoskeleton 40, 160-173.
    • (1998) Cell Motil. Cytoskeleton , vol.40 , pp. 160-173
    • Ruthel, G.1    Banker, G.2
  • 29
    • 0032999918 scopus 로고    scopus 로고
    • Role of moving growth cone-like "wave" structures in the outgrowth of cultured hippocampal axons and dendrites
    • Ruthel, G., and Banker, G. (1999). Role of moving growth cone-like "wave" structures in the outgrowth of cultured hippocampal axons and dendrites. J. Neurobiol. 39, 97-106.
    • (1999) J. Neurobiol. , vol.39 , pp. 97-106
    • Ruthel, G.1    Banker, G.2
  • 31
    • 0021210339 scopus 로고
    • A tumor promoter induces rapid and coordinated reorganization of actin and vinculin in cultured cells
    • Schliwa, M., Nakamura, T., Porter, K.R., and Euteneuer, U. (1984). A tumor promoter induces rapid and coordinated reorganization of actin and vinculin in cultured cells. J. Cell Biol. 99, 1045-1059.
    • (1984) J. Cell Biol. , vol.99 , pp. 1045-1059
    • Schliwa, M.1    Nakamura, T.2    Porter, K.R.3    Euteneuer, U.4
  • 32
    • 0026023289 scopus 로고
    • Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
    • Soriano, P., Montgomery, C., Geske, R., and Bradley, A. (1991). Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64, 693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 33
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer, S.M., and Hinshaw, J.E. (1998). Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell 93, 1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 34
    • 0029858150 scopus 로고    scopus 로고
    • c-Cbl is downstream of c-Src in a signaling pathway necessary for bone resorption
    • Tanaka, S., Amling, M., Neff, L., Peyman, A., Uhlmann, E., Levy, J.B., and Baron, R. (1996). c-Cbl is downstream of c-Src in a signaling pathway necessary for bone resorption. Nature 383, 528-531.
    • (1996) Nature , vol.383 , pp. 528-531
    • Tanaka, S.1    Amling, M.2    Neff, L.3    Peyman, A.4    Uhlmann, E.5    Levy, J.B.6    Baron, R.7
  • 35
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone, G., Cirillo, D., Giancotti, F.G., Comoglio, P.M., and Marchisio, P.C. (1985). Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 159, 141-157.
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 36
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A.V., Lamaze, C., and Schmid, S.L. (1996). Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 37
    • 0031696485 scopus 로고    scopus 로고
    • Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1
    • Weed, S., Du, Y., and Parsons, J. (1998). Translocation of cortactin to the cell periphery is mediated by the small GTPase Rac1. J. Cell Sci. 111, 2433-2443.
    • (1998) J. Cell Sci. , vol.111 , pp. 2433-2443
    • Weed, S.1    Du, Y.2    Parsons, J.3
  • 38
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • Weed, S.A., Karginov, A.V., Schafer, D.A., Weaver, A.M., Kinley, A.W., Cooper, J.A., and Parsons, J.T. (2000). Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151, 29-40.
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 39
    • 0033231935 scopus 로고    scopus 로고
    • The world according to Arp: Regulation of actin nucleation by the Arp2/3 complex
    • Welch, M.D. (1999). The world according to Arp: regulation of actin nucleation by the Arp2/3 complex. Trends Cell Biol. 9, 423-427.
    • (1999) Trends Cell Biol. , vol.9 , pp. 423-427
    • Welch, M.D.1
  • 40
    • 0034282711 scopus 로고    scopus 로고
    • Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold
    • Westphal, R.S., Soderling, S.H., Alto, N.M., Langeberg, L.K., and Scott, J.D. (2000). Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold. EMBO J. 19, 4589-4600.
    • (2000) EMBO J. , vol.19 , pp. 4589-4600
    • Westphal, R.S.1    Soderling, S.H.2    Alto, N.M.3    Langeberg, L.K.4    Scott, J.D.5
  • 41
    • 0027419589 scopus 로고
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120, 1417-1426.
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2


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