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Volumn 23, Issue 19, 2003, Pages 6809-6822

Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL TOXIN; CYTOTOXIC NECROTIZING FACTOR 1; ENZYME ACTIVATOR; F ACTIN; GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42; RAC PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; VINCULIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 0141669167     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.19.6809-6822.2003     Document Type: Article
Times cited : (172)

References (58)
  • 1
    • 0028964295 scopus 로고
    • ADP-ribosylation of Rho enhances adhesion of U937 cells to fibronectin via the alpha 5 beta 1 integrin receptor
    • Aepfelbacher, M. 1995. ADP-ribosylation of Rho enhances adhesion of U937 cells to fibronectin via the alpha 5 beta 1 integrin receptor. FEBS Lett. 363:78-80.
    • (1995) FEBS Lett. , vol.363 , pp. 78-80
    • Aepfelbacher, M.1
  • 2
    • 0028328250 scopus 로고
    • Spreading of differentiating human monocytes is associated with a major increase in membrane-bound CDC42
    • Aepfelbacher, M., F. Vauti, P. C. Weber, and J. A. Glomset. 1994. Spreading of differentiating human monocytes is associated with a major increase in membrane-bound CDC42. Proc. Natl. Acad. Sci. USA 91:4263-4267.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4263-4267
    • Aepfelbacher, M.1    Vauti, F.2    Weber, P.C.3    Glomset, J.A.4
  • 3
    • 0022633123 scopus 로고
    • Primary culture of endothelial cells from atherosclerotic human aorta. Part 1. Identification, morphological and ultrastructural characteristics of two endothelial cell subpopulations
    • Antonov, A. S., M. A. Nikolaeva, T. S. Klueva, A. Romanov Yu, V. R. Babaev, V. B. Bystrevskaya, N. A. Perov, V. S. Repin, and V. N. Smirnov. 1986. Primary culture of endothelial cells from atherosclerotic human aorta. Part 1. Identification, morphological and ultrastructural characteristics of two endothelial cell subpopulations. Atherosclerosis 59:1-19.
    • (1986) Atherosclerosis , vol.59 , pp. 1-19
    • Antonov, A.S.1    Nikolaeva, M.A.2    Klueva, T.S.3    Romanov, Yu.A.4    Babaev, V.R.5    Bystrevskaya, V.B.6    Perov, N.A.7    Repin, V.S.8    Smirnov, V.N.9
  • 4
    • 0035883040 scopus 로고    scopus 로고
    • Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation
    • Burns, S., A. J. Thrasher, M. P. Blundell, L. Machesky, and G. E. Jones. 2001. Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation. Blood 98:1142-1149.
    • (2001) Blood , vol.98 , pp. 1142-1149
    • Burns, S.1    Thrasher, A.J.2    Blundell, M.P.3    Machesky, L.4    Jones, G.E.5
  • 5
    • 0034695921 scopus 로고    scopus 로고
    • Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength
    • Chellaiah, M., N. Kizer, M. Silva, U. Alvarez, D. Kwiatkowski, and K. A. Hruska. 2000. Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength. J. Cell Biol. 148:665-678.
    • (2000) J. Cell Biol. , vol.148 , pp. 665-678
    • Chellaiah, M.1    Kizer, N.2    Silva, M.3    Alvarez, U.4    Kwiatkowski, D.5    Hruska, K.A.6
  • 7
    • 0024414571 scopus 로고
    • Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells
    • Chen, W. T. 1989. Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells. J. Exp Zool. 251:167-185.
    • (1989) J. Exp Zool. , vol.251 , pp. 167-185
    • Chen, W.T.1
  • 8
    • 0033105764 scopus 로고    scopus 로고
    • Synergistic activation of JNK/SAPK by interleukin-1 and platelet-derived growth factor is independent of Rac and Cdc42
    • Davis, W., L. R. Stephens, P. T. Hawkins, and J. Saklatvala. 1999. Synergistic activation of JNK/SAPK by interleukin-1 and platelet-derived growth factor is independent of Rac and Cdc42. Biochem. J. 338:387-392.
    • (1999) Biochem. J. , vol.338 , pp. 387-392
    • Davis, W.1    Stephens, L.R.2    Hawkins, P.T.3    Saklatvala, J.4
  • 9
    • 0032899885 scopus 로고    scopus 로고
    • Cytoskeletal and adhesive structural polarizations accompany IL-13-induced human macrophage fusion
    • DeFife, K. M., C. R. Jenney, E. Colton, and J. M. Anderson. 1999. Cytoskeletal and adhesive structural polarizations accompany IL-13-induced human macrophage fusion. J. Histochem. Cytochem. 47:65-74.
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 65-74
    • DeFife, K.M.1    Jenney, C.R.2    Colton, E.3    Anderson, J.M.4
  • 11
    • 0031806711 scopus 로고    scopus 로고
    • Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes
    • D'Souza-Schorey, C., B. Boettner, and L. Van Aelst. 1998. Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes. Mol. Cell. Biol. 18:3936-3946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3936-3946
    • D'Souza-Schorey, C.1    Boettner, B.2    Van Aelst, L.3
  • 12
    • 0035313804 scopus 로고    scopus 로고
    • Multiple roles for Cdc42 in cell regulation
    • Erickson, J. W., and R. A. Cerione. 2001. Multiple roles for Cdc42 in cell regulation. Curr. Opin. Cell Biol. 13:153-157.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 153-157
    • Erickson, J.W.1    Cerione, R.A.2
  • 13
    • 0029088441 scopus 로고
    • Escherichia coli cytotoxic necrotizing factor 1: Evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase
    • Fiorentini, C., G. Donelli, P. Matarrese, A. Fabbri, S. Paradisi, and P. Boquet. 1995. Escherichia coli cytotoxic necrotizing factor 1: evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase. Infect. Immun. 63:3936-3944.
    • (1995) Infect. Immun. , vol.63 , pp. 3936-3944
    • Fiorentini, C.1    Donelli, G.2    Matarrese, P.3    Fabbri, A.4    Paradisi, S.5    Boquet, P.6
  • 15
    • 0031014969 scopus 로고    scopus 로고
    • Rapid Ca2+-mediated activation of Rap1 in human platelets
    • Franke, B., J. W. Akkerman, and J. L. Bos. 1997. Rapid Ca2+-mediated activation of Rap1 in human platelets. EMBO J. 16:252-259.
    • (1997) EMBO J. , vol.16 , pp. 252-259
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 16
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht, F., and M. Way. 2001. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11:30-38.
    • (2001) Trends Cell Biol , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 17
    • 0024728927 scopus 로고
    • Ultrastructure and gold-immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells
    • Gavazzi, I., M. V. Nermut, and P. C. Marchisio. 1989. Ultrastructure and gold-immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells. J. Cell Sci. 94:85-99.
    • (1989) J. Cell Sci. , vol.94 , pp. 85-99
    • Gavazzi, I.1    Nermut, M.V.2    Marchisio, P.C.3
  • 19
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin, N. A., and A. Hall. 1995. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131:1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 20
    • 0017081429 scopus 로고
    • Characterization of the collagen synthesized by endothelial cells in culture
    • Howard, B. V., E. J. Macarak, D. Gunson, and N. A. Kefalides. 1976. Characterization of the collagen synthesized by endothelial cells in culture. Proc. Natl. Acad. Sci. USA 73:2361-2364.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2361-2364
    • Howard, B.V.1    Macarak, E.J.2    Gunson, D.3    Kefalides, N.A.4
  • 21
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim, A. S., L. T. Kakalis, N. Abdul-Manan, G. A. Liu, and M. K. Rosen. 2000. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404:151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 22
    • 0035824573 scopus 로고    scopus 로고
    • Redox regulation of human Rac1 stability by the proteasome in human aortic endothelial cells
    • Kovacic, H. N., K. Irani, and P. J. Goldschmidt-Clermont. 2001. Redox regulation of human Rac1 stability by the proteasome in human aortic endothelial cells. J. Biol. Chem. 276:45856-45861.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45856-45861
    • Kovacic, H.N.1    Irani, K.2    Goldschmidt-Clermont, P.J.3
  • 23
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • Lamarche, N., N. Tapon, L. Stowers, P. D. Burbelo, P. Aspenstrom, T. Bridges, J. Chant, and A. Hall. 1996. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 87:519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
  • 24
    • 0036070562 scopus 로고    scopus 로고
    • Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac
    • Lerm, M., M. Pop, G. Fritz, K. Aktories, and G. Schmidt. 2002. Proteasomal degradation of cytotoxic necrotizing factor 1-activated Rac. Infect. Immun. 70:4053-4058.
    • (2002) Infect. Immun. , vol.70 , pp. 4053-4058
    • Lerm, M.1    Pop, M.2    Fritz, G.3    Aktories, K.4    Schmidt, G.5
  • 25
    • 0032909858 scopus 로고    scopus 로고
    • Deamidation of Cdc42 and Rac by Escherichia coli cytotoxic necrotizing factor1: Activation of c-Jun N-terminal kinase in Hela cells
    • Lerm, M., J. Selzer, A. Hoffmeyer, U. R. Rapp, K. Aktories, and G. Schmidt. 1999. Deamidation of Cdc42 and Rac by Escherichia coli cytotoxic necrotizing factor1: activation of c-Jun N-terminal kinase in Hela cells. Infect. Immun. 67:496-503.
    • (1999) Infect. Immun. , vol.67 , pp. 496-503
    • Lerm, M.1    Selzer, J.2    Hoffmeyer, A.3    Rapp, U.R.4    Aktories, K.5    Schmidt, G.6
  • 26
    • 0033570021 scopus 로고    scopus 로고
    • Localization of the PAK1-WASP-, and IQGAP1-specifying regions of Cdc42
    • Li, R., B. Debreceni, B. Jia, Y. Goa, G. Tigyi, and Y. Zheng. 1999. Localization of the PAK1-, WASP-, and IQGAP1-specifying regions of Cdc42. J. Biol. Chem. 274:29648-29654.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29648-29654
    • Li, R.1    Debreceni, B.2    Jia, B.3    Goa, Y.4    Tigyi, G.5    Zheng, Y.6
  • 27
    • 0033560932 scopus 로고    scopus 로고
    • Distinct roles for the small GTPases Cdc42 and Rho in endothelial responses to shear stress
    • Li, S., B. P. Chen, N. Azuma, Y. L. Hu, S. Z. Wu, B. E. Sumpio, J. Y. Shyy, and S. Chien. 1999. Distinct roles for the small GTPases Cdc42 and Rho in endothelial responses to shear stress. J. Clin. Investig. 103:1141-1150.
    • (1999) J. Clin. Investig. , vol.103 , pp. 1141-1150
    • Li, S.1    Chen, B.P.2    Azuma, N.3    Hu, Y.L.4    Wu, S.Z.5    Sumpio, B.E.6    Shyy, J.Y.7    Chien, S.8
  • 28
    • 0033578374 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein regulates podosomes in primary human macrophages
    • Linder, S., D. Nelson, M. Weiss, and M. Aepfelbacher. 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
  • 29
    • 0021166977 scopus 로고
    • Immunofluorescence localization of phosphotyrosine containing proteins in RSV-transformed mouse fibroblasts
    • Marchisio, P. C., M. F. Di Renzo, and P. M. Comoglio. 1984. Immunofluorescence localization of phosphotyrosine containing proteins in RSV-transformed mouse fibroblasts. Exp. Cell Res. 154:112-124.
    • (1984) Exp. Cell Res. , vol.154 , pp. 112-124
    • Marchisio, P.C.1    Di Renzo, M.F.2    Comoglio, P.M.3
  • 31
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D., J. Silletti, G. Murphy, P. D'Eustachio, M. Rush, and M. R. Philips. 2001. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152:111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 32
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani, K., H. Miki, H. He, H. Maruta, and T. Takenawa. 2002. Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res. 62:669-674.
    • (2002) Cancer Res. , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenawa, T.5
  • 34
    • 0036024589 scopus 로고    scopus 로고
    • Constitutive active GTPases Rac and Cdc42 are associated with endoreplication in PAE cells
    • Muris, D., T. Verschoor, N. Divecha, and R. Michalides. 2002. Constitutive active GTPases Rac and Cdc42 are associated with endoreplication in PAE cells. Eur. J. Cancer 38:1775.
    • (2002) Eur. J. Cancer , vol.38 , pp. 1775
    • Muris, D.1    Verschoor, T.2    Divecha, N.3    Michalides, R.4
  • 35
    • 0037341905 scopus 로고    scopus 로고
    • Redox-dependent downregulation of Rho by Rac
    • Nimnual, A. S., L. J. Taylor, and D. Bar-Sagi. 2003. Redox-dependent downregulation of Rho by Rac. Nat. Cell Biol. 5:236-241.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 236-241
    • Nimnual, A.S.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 36
    • 0024341210 scopus 로고
    • The podosomes of Rous sarcoma virus transformed chondrocytes show a peculiar ultrastructural organization
    • Nitsch, L., E. Gionti, R. Cancedda, and P. C. Marchisio. 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
  • 37
    • 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 A. Hall. 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
  • 38
    • 0035253608 scopus 로고    scopus 로고
    • Trophoblast giant-cell differentiation involves changes in cytoskeleton and cell motility
    • Parast, M. M., S. Aeder, and A. E. Sutherland. 2001. Trophoblast giant-cell differentiation involves changes in cytoskeleton and cell motility. Dev. Biol. 230:43-60.
    • (2001) Dev. Biol. , vol.230 , pp. 43-60
    • Parast, M.M.1    Aeder, S.2    Sutherland, A.E.3
  • 39
    • 0034865951 scopus 로고    scopus 로고
    • Podosomes in osteoclast-like cells: Structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase 2 (Pyk2) and integrin alphaVbeta3
    • Pfaff, M., and P. Jurdic. 2001. Podosomes in osteoclast-like cells: structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase 2 (Pyk2) and integrin alphaVbeta3. J. Cell Sci. 114:2775-2786.
    • (2001) J. Cell Sci. , vol.114 , pp. 2775-2786
    • Pfaff, M.1    Jurdic, P.2
  • 40
    • 0032841725 scopus 로고    scopus 로고
    • Activation of the small GTPase Cdc42 by the inflammatory cytokines TNF(alpha) and IL-1, and by the Epstein-Barr virus transforming protein LMP1
    • Puls, A., A. G. Eliopoulos, C. D. Nobes, T. Bridges, L. S. Young, and A. Hall. 1999. Activation of the small GTPase Cdc42 by the inflammatory cytokines TNF(alpha) and IL-1, and by the Epstein-Barr virus transforming protein LMP1. J. Cell Sci. 112:2983-2992.
    • (1999) J. Cell Sci. , vol.112 , pp. 2983-2992
    • Puls, A.1    Eliopoulos, A.G.2    Nobes, C.D.3    Bridges, T.4    Young, L.S.5    Hall, A.6
  • 41
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., W. B. Kiosses, and M. A. Schwartz. 1999. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 42
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner, K., A. Hall, and J. V. Small. 1999. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9:640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 43
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai, E., and C. J. Marshall. 2002. ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat. Cell Biol. 4:408-415.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 44
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac1 signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • Sander, E., S. V. Delft, J. T. Klooster, T. Reid, R. V. D. Kammen, F. Michiels, and J. Collard. 1998. Matrix-dependent Tiam1/Rac1 signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143:1385-1398.
    • (1998) J. Cell Biol. , vol.143 , pp. 1385-1398
    • Sander, E.1    Delft, S.V.2    Klooster, J.T.3    Reid, T.4    Kammen, R.V.D.5    Michiels, F.6    Collard, J.7
  • 45
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: Reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E. E., J. P. ten Klooster, S. van Delft, R. A. van der Kammen, and J. G. Collard. 1999. Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147:1009-1022.
    • (1999) J. Cell Biol. , vol.147 , pp. 1009-1022
    • Sander, E.E.1    Ten Klooster, J.P.2    Van Delft, S.3    Van der Kammen, R.A.4    Collard, J.G.5
  • 46
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility
    • Sanjay, A., A. Houghton, L. Neff, E. DiDomenico, C. Bardelay, E. Antoine, J. Levy, J. Gailit, D. Bowtell, W. C. Horne, and R. Baron. 2001. Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility. J. Cell Biol. 152:181-195.
    • (2001) J. Cell Biol. , vol.152 , pp. 181-195
    • Sanjay, A.1    Houghton, A.2    Neff, L.3    DiDomenico, E.4    Bardelay, C.5    Antoine, E.6    Levy, J.7    Gailit, J.8    Bowtell, D.9    Horne, W.C.10    Baron, R.11
  • 47
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt, G., P. Sehr, M. Wilm, J. Selzer, M. Mann, and K. Aktories. 1997. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387:725-729.
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 48
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
    • Sebbagh, M., C. Renvoize, J. Hamelin, N. Riche, J. Bertoglio, and J. Breard. 2001. Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat. Cell Biol. 3:346-352.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 346-352
    • Sebbagh, M.1    Renvoize, C.2    Hamelin, J.3    Riche, N.4    Bertoglio, J.5    Breard, J.6
  • 50
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., J. M. Derry, B. Karlak, S. Jiang, V. Lemahieu, F. Mccormick, U. Francke, and A. Abo. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    Mccormick, F.6    Francke, U.7    Abo, A.8
  • 51
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • Tarone, G., D. Cirillo, F. Giancotti, P. Comoglio, and P. Marchisio. 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.3    Comoglio, P.4    Marchisio, P.5
  • 52
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 53
    • 0037016718 scopus 로고    scopus 로고
    • The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation
    • Vetterkind, S., H. Miki, T. Takenawa, I. Klawitz, K. H. Scheidtmann, and U. Preuss. 2002. The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation. J. Biol. Chem. 277:87-95.
    • (2002) J. Biol. Chem. , vol.277 , pp. 87-95
    • Vetterkind, S.1    Miki, H.2    Takenawa, T.3    Klawitz, I.4    Scheidtmann, K.H.5    Preuss, U.6
  • 54
    • 0037096160 scopus 로고    scopus 로고
    • Distinct signals via Rho GTPases and Src drive shape changes by thrombin and sphingosine-1-phosphate in endothelial cells
    • Vouret-Craviari, V., C. Bourcier, E. Boulter, and E. Van Obberghen-Schilling. 2002. Distinct signals via Rho GTPases and Src drive shape changes by thrombin and sphingosine-1-phosphate in endothelial cells. J. Cell Sci. 115:2475-2484.
    • (2002) J. Cell Sci. , vol.115 , pp. 2475-2484
    • Vouret-Craviari, V.1    Bourcier, C.2    Boulter, E.3    Van Obberghen-Schilling, E.4
  • 55
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M. D., A. Iwamatsu, and T. J. Mitchison. 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385:265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 56
    • 0034331308 scopus 로고    scopus 로고
    • Laminin-1 activates Cdc42 in the mechanism of laminin-1-mediated neurite outgrowth
    • Weston, C. A., L. Anova, C. Rialas, J. M. Prives, and B. S. Weeks. 2000. Laminin-1 activates Cdc42 in the mechanism of laminin-1-mediated neurite outgrowth. Exp. Cell Res. 260:374-378.
    • (2000) Exp. Cell Res. , vol.260 , pp. 374-378
    • Weston, C.A.1    Anova, L.2    Rialas, C.3    Prives, J.M.4    Weeks, B.S.5
  • 57
    • 0035374569 scopus 로고    scopus 로고
    • RhoA inhibits the nerve growth factor-induced Rac1 activation through Rho-associated kinase-dependent pathway
    • Yamaguchi, Y., H. Katoh, H. Yasui, K. Mori, and M. Negishi. 2001. RhoA inhibits the nerve growth factor-induced Rac1 activation through Rho-associated kinase-dependent pathway. J. Biol. Chem. 276:18977-18983.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18977-18983
    • Yamaguchi, Y.1    Katoh, H.2    Yasui, H.3    Mori, K.4    Negishi, M.5


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