메뉴 건너뛰기




Volumn 5, Issue 3, 2003, Pages 195-204

RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; GUANOSINE TRIPHOSPHATASE; METHENAMINE; PROTEIN TYROSINE KINASE; RHO FACTOR;

EID: 0037341806     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb935     Document Type: Article
Times cited : (180)

References (54)
  • 1
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosts and molecular sorting
    • Mellman, I. Endocytosts and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625 (1996).
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 2
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kobler, E. & Riezman, H. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12, 2855-2862 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kobler, E.1    Riezman, H.2
  • 3
    • 0034139820 scopus 로고    scopus 로고
    • Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells
    • Fujimoto, L. M., Roth, R., Heuser, J. E. & Schmid, S. L. Actin assembly plays a variable, but not obligatory role in receptor-mediated endocytosis in mammalian cells. Traffic 1, 161-171 (2000).
    • (2000) Traffic , vol.1 , pp. 161-171
    • Fujimoto, L.M.1    Roth, R.2    Heuser, J.E.3    Schmid, S.L.4
  • 4
    • 0035898659 scopus 로고    scopus 로고
    • Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis
    • Buss, F., Arden, S. D., Lindsay, M., Luzio, J. P. & Kendrick-Jones, J. Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis. EMBO J. 20, 3676-3684 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3676-3684
    • Buss, F.1    Arden, S.D.2    Lindsay, M.3    Luzio, J.P.4    Kendrick-Jones, J.5
  • 5
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach, A., Louvard, D. & Coudrier, E. Actin filaments facilitate two steps of endocytosis. J. Cell Sci. 109, 457-465 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 6
    • 0032897519 scopus 로고    scopus 로고
    • Association of myosin I α with endosomes and lysosomes in mammalian cells
    • Raposo, G. et al. Association of myosin I α with endosomes and lysosomes in mammalian cells. Mol. Biol. Cell 10, 1477-1494 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1477-1494
    • Raposo, G.1
  • 7
    • 0035145716 scopus 로고    scopus 로고
    • Actin filament nucleation by endosomes, lysosomes and secretory vesicles
    • Taunton, J. Actin filament nucleation by endosomes, lysosomes and secretory vesicles. Curr. Opin. Cell Biol. 13, 85-91 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 85-91
    • Taunton, J.1
  • 8
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni, R. & Kreis, T. E. Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105, 1253-1265 (1987).
    • (1987) J. Cell Biol. , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 9
    • 0027222916 scopus 로고
    • Isolation of a temperature-sensitive variant Chinese hamster ovary cell line with a morphologically altered endocytic recycling compartment
    • McGraw, T. E., Dunn, K. W. & Maxfield, F. R. Isolation of a temperature-sensitive variant Chinese hamster ovary cell line with a morphologically altered endocytic recycling compartment. J. Cell Physiol. 155, 579-594 (1993).
    • (1993) J. Cell Physiol. , vol.155 , pp. 579-594
    • McGraw, T.E.1    Dunn, K.W.2    Maxfield, F.R.3
  • 11
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento, F., Emans, N., Griffiths, G. & Gruenberg, J. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 123, 1373-1387 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 12
    • 0025029828 scopus 로고
    • Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel, M., Parton, R., Kuznetsov, S. A., Schroer, T. & Gruenberg, J. Microtubule- and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62, 719-731 (1990).
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.4    Gruenberg, J.5
  • 14
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley, A. J. Rho proteins: linking signaling with membrane trafficking. Traffic 2, 303-310 (2001).
    • (2001) Traffic , vol.2 , pp. 303-310
    • Ridley, A.J.1
  • 15
  • 16
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A. & Mellman, I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nature Cell Biol. 1, 8-13 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 17
    • 10544237679 scopus 로고    scopus 로고
    • Endosome dynamics regulated by a novel rho protein
    • Murphy, C. et al. Endosome dynamics regulated by a novel rho protein. Nature 384, 427-432 (1996).
    • (1996) Nature , vol.384 , pp. 427-432
    • Murphy, C.1
  • 18
    • 0033539150 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor traffic by the small GTPase RhoB
    • Gampel, A., Parker, P. J. & Mellor, H. Regulation of epidermal growth factor receptor traffic by the small GTPase RhoB. Curr. Biol. 9, 955-958 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 955-958
    • Gampel, A.1    Parker, P.J.2    Mellor, H.3
  • 19
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A. L. & Hall, A. Rho GTPases and their effector proteins. Biochem J. 348, 241-255 (2000).
    • (2000) Biochem J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 20
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, M. et al. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122 (1997).
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1
  • 21
    • 10544228528 scopus 로고    scopus 로고
    • Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Kohno, H. et al. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15, 6060-6068 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6060-6068
    • Kohno, H.1
  • 22
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7
    • Alberts, A. S., Bouquin, N., Johnston, L. H. & Treisman, R. Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7. J. Biol. Chem. 273, 8616-8622 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 23
    • 0030911424 scopus 로고    scopus 로고
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N. et al. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 24
    • 0035824618 scopus 로고    scopus 로고
    • The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription front the serum response element
    • Westendorf, J. J. The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription front the serum response element. J. Biol. Chem. 276, 46453-46459 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46453-46459
    • Westendorf, J.J.1
  • 25
    • 0033816998 scopus 로고    scopus 로고
    • FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages
    • Yayoshi-Yamamoto, S., Taniuchi, I. & Watanabe, T. FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. Mol. Cell Biol. 20, 6872-6881 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6872-6881
    • Yayoshi-Yamamoto, S.1    Taniuchi, I.2    Watanabe, T.3
  • 26
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman, S. FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111-115 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 27
    • 0034684965 scopus 로고    scopus 로고
    • Formin family proteins in cytoskeletal control
    • Tanaka, K. Formin family proteins in cytoskeletal control. Biochem. Biophys. Res. Commun. 267, 479-481 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 479-481
    • Tanaka, K.1
  • 28
    • 0033635022 scopus 로고    scopus 로고
    • Artemis: Sequence visualization and annotation
    • Rutherford, K. et al. Artemis: sequence visualization and annotation. Bioinformatics 16, 944-945 (2000).
    • (2000) Bioinformatics , vol.16 , pp. 944-945
    • Rutherford, K.1
  • 29
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Chistoforidis, S., McBride, H. M., Burgoyne, R., D. & Zerial, M. The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621-625 (1999).
    • (1999) Nature , vol.397 , pp. 621-625
    • Chistoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 30
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe, N., Kato, T., Fujita, A., Ishizaki, T. & Narumiya, S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nature Cell Biel. 1, 136-143 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 31
    • 0034950065 scopus 로고    scopus 로고
    • Dual function of RhoD in vesicular movement and cell motility
    • Murphy, C. et al. Dual function of RhoD in vesicular movement and cell motility. Eur. J. Cell Biol. 80, 391-398 (2001).
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 391-398
    • Murphy, C.1
  • 32
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen, B., De Renzis, S., Nielsen, E., Rietdorf, J. & Zerial, M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J. Cell Biol. 149, 901-914 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 901-914
    • Sonnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 33
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S. M. et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498 (2001).
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1
  • 34
    • 0035141074 scopus 로고    scopus 로고
    • Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1
    • Ishizaki, T. et al. Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nature Cell Biol. 3, 8-14 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 8-14
    • Ishizaki, T.1
  • 35
    • 0012644537 scopus 로고    scopus 로고
    • Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling
    • Tominaga, T. et al. Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling. Mol. Cell 5, 13-25 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 13-25
    • Tominaga, T.1
  • 36
    • 0026611047 scopus 로고
    • Association of p60c-src with endosomal membranes in mammalian fibroblasts
    • Kaplan, K. B., Swedlow, J. R., Varmus, H. E. & Morgan, D. O. Association of p60c-src with endosomal membranes in mammalian fibroblasts. J. Cell Biol. 118, 321-133 (1992).
    • (1992) J. Cell Biol. , vol.118 , pp. 133-321
    • Kaplan, K.B.1    Swedlow, J.R.2    Varmus, H.E.3    Morgan, D.O.4
  • 37
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A. & Soriano, P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459-2471 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 38
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline, D. et al. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J. Cell Biol. 153, 1175-1186 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1
  • 39
    • 0034941053 scopus 로고    scopus 로고
    • pp60(c-src) and related tyrosine kinases: A role in the assembly and reorganization of matrix adhesions
    • Volberg, T., Romer, L., Zamir, E. & Geiger, B. pp60(c-src) and related tyrosine kinases: a role in the assembly and reorganization of matrix adhesions. J. Cell Sci. 114, 2279-2289 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 2279-2289
    • Volberg, T.1    Romer, L.2    Zamir, E.3    Geiger, B.4
  • 40
    • 17344369363 scopus 로고    scopus 로고
    • A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: Evidence for conserved function in oogenesis and implications for human sterility
    • Bione, S. et al. A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: evidence for conserved function in oogenesis and implications for human sterility. Am. J. Hum. Genet. 62, 533-541 (1998).
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 533-541
    • Bione, S.1
  • 41
    • 0034759486 scopus 로고    scopus 로고
    • Characterization of functional domains of mDia1, a link between the small GTPase Rho and the actin cytoskeleton
    • Krebs, A., Rothkegel, M., Klar, M. & Jockusch, B. M. Characterization of functional domains of mDia1, a link between the small GTPase Rho and the actin cytoskeleton. J. Cell Sci. 114, 3663-3672 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3663-3672
    • Krebs, A.1    Rothkegel, M.2    Klar, M.3    Jockusch, B.M.4
  • 42
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C. & Bretscher, A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nature Cell Biol. 4, 32-41 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 43
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • Pruyne, D. et al. Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615 (2002).
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1
  • 44
    • 0034907213 scopus 로고    scopus 로고
    • mDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A. F., Cook, T. A., Alberts, A. S. & Gundersen, G. G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nature Cell Biol. 3, 723-729 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 45
    • 0030460431 scopus 로고    scopus 로고
    • Molecular interaction between limb deformity proteins (formins) and Src family kinases
    • Uetz, P., Fumagalli, S., James, D. & Zeller, R. Molecular interaction between limb deformity proteins (formins) and Src family kinases. J. Biol. Chem. 271, 33525-33530 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 33525-33530
    • Uetz, P.1    Fumagalli, S.2    James, D.3    Zeller, R.4
  • 46
    • 0025940103 scopus 로고
    • Identification and characterization of a novel cytoskeleton-associated pp60src substrate
    • Wu, H., Reynolds, A. B., Kanner, S. B., Vines, R. R. & Parsons, J. T. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol. Cell Biol. 11, 5113-5124 (1991).
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5113-5124
    • Wu, H.1    Reynolds, A.B.2    Kanner, S.B.3    Vines, R.R.4    Parsons, J.T.5
  • 47
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno, T. et al. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nature Cell Biol. 3, 259-266 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 259-266
    • Uruno, T.1
  • 48
    • 0033561496 scopus 로고    scopus 로고
    • Small GTPase RhoD suppresses cell migration and cytokinesis
    • Tsubakimoto, K. et al. Small GTPase RhoD suppresses cell migration and cytokinesis. Oncogene 18, 2431-2440 (1999).
    • (1999) Oncogene , vol.18 , pp. 2431-2440
    • Tsubakimoto, K.1
  • 49
    • 0027183419 scopus 로고
    • Membrane partitioning during cell division
    • Warren, G. Membrane partitioning during cell division. Annu. Rev. Biochem. 62, 323-348 (1993).
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 323-348
    • Warren, G.1
  • 50
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells
    • Kato, T. et al. Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J. Cell Sci. 114, 775-784 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 775-784
    • Kato, T.1
  • 52
    • 0034427027 scopus 로고    scopus 로고
    • Purification and identification of novel Rab effectors using affinity chromatography
    • Christoforidis, S. & Zerial, M. Purification and identification of novel Rab effectors using affinity chromatography. Methods 20, 403-410 (2000).
    • (2000) Methods , vol.20 , pp. 403-410
    • Christoforidis, S.1    Zerial, M.2
  • 54
    • 0032686937 scopus 로고    scopus 로고
    • Feature point tracking for incomplete trajectories
    • Chetverikov, D. & Verestói, J. Feature point tracking for incomplete trajectories. Computing 62, 321-338 (1999).
    • (1999) Computing , vol.62 , pp. 321-338
    • Chetverikov, D.1    Verestói, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.