메뉴 건너뛰기




Volumn 25, Issue 5, 2005, Pages 1680-1695

Spatially distinct binding of Cdc42 to PAK1 and N-WASP in breast carcinoma cells

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATE; NUCLEOTIDE; PROTEIN CDC42; PROTEIN P21; RAB PROTEIN; THREONINE; TRANSFERRIN RECEPTOR; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 20044376673     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.5.1680-1695.2005     Document Type: Article
Times cited : (81)

References (62)
  • 2
    • 0142073731 scopus 로고    scopus 로고
    • Interaction of fascin and protein kinase C{alpha}: A novel intersection in cell adhesion and motility
    • Anilkumar, N., M. Parsons, R. Monk, T. Ng, and J. C. Adams. 2003. Interaction of fascin and protein kinase C{alpha}: a novel intersection in cell adhesion and motility. EMBO J. 22:5390-5402.
    • (2003) EMBO J. , vol.22 , pp. 5390-5402
    • Anilkumar, N.1    Parsons, M.2    Monk, R.3    Ng, T.4    Adams, J.C.5
  • 3
    • 0029680639 scopus 로고    scopus 로고
    • Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom, P., U. Lindberg, and A. Hall. 1996. Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr. Biol. 6:70-75.
    • (1996) Curr. Biol. , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 4
    • 0024676128 scopus 로고
    • A second generation global analysis program for the recovery of complex inhomogeneous fluorescence decay kinetics
    • Beechem, J. M. 1989. A second generation global analysis program for the recovery of complex inhomogeneous fluorescence decay kinetics. Chem. Phys. Lipids 50:237-251.
    • (1989) Chem. Phys. Lipids , vol.50 , pp. 237-251
    • Beechem, J.M.1
  • 5
    • 0022777385 scopus 로고
    • Global analysis of fluorescence decay: Applications to some unusual experimental and theoretical studies
    • Beechem, J. M., and L. Brand. 1986. Global analysis of fluorescence decay: applications to some unusual experimental and theoretical studies. Photochem. Photobiol. 44:323-329.
    • (1986) Photochem. Photobiol. , vol.44 , pp. 323-329
    • Beechem, J.M.1    Brand, L.2
  • 6
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • Brown, M. C., K. A. West, and C. E. Turner. 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.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 8
    • 0033862387 scopus 로고    scopus 로고
    • P190-B, a Rho-GTPase-activating protein, is differentially expressed in terminal end buds and breast cancer
    • Chakravarty, G., D. Roy, M. Gonzales, J. Gay, A. Contreras, and J. M. Rosen. 2000. P190-B, a Rho-GTPase-activating protein, is differentially expressed in terminal end buds and breast cancer. Cell Growth Differ. 11:343-354.
    • (2000) Cell Growth Differ. , vol.11 , pp. 343-354
    • Chakravarty, G.1    Roy, D.2    Gonzales, M.3    Gay, J.4    Contreras, A.5    Rosen, J.M.6
  • 9
    • 0037452977 scopus 로고    scopus 로고
    • A WASp homolog powers actin polymerization-dependent motility of endosomes in vivo
    • Chang, F. S., C. J. Stefan, and K. J. Blumer. 2003. A WASp homolog powers actin polymerization-dependent motility of endosomes in vivo. Curr. Biol. 13:455-463.
    • (2003) Curr. Biol. , vol.13 , pp. 455-463
    • Chang, F.S.1    Stefan, C.J.2    Blumer, K.J.3
  • 10
    • 0035907296 scopus 로고    scopus 로고
    • The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
    • Chong, C., L. Tan, L. Lim, and E. Manser. 2001. The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity. J. Biol. Chem. 276:17347-17353.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17347-17353
    • Chong, C.1    Tan, L.2    Lim, L.3    Manser, E.4
  • 11
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • Daub, H., K. Gevaert, J. Vandekerckhove, A. Sobel, and A. Hall. 2001. Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16. J. Biol. Chem. 276:1677-1680.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 12
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., R. Rohatgi, A. V. Podtelejnikov, M. Mann, and M. W. Kirschner. 2002. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418:790-793.
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 13
    • 0032561355 scopus 로고    scopus 로고
    • Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation
    • Frost, J. A., A. Khokhlatchev, S. Stippec, M. A. White, and M. H. Cobb. 1998. Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation. J. Biol. Chem. 273:28191-28198.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28191-28198
    • Frost, J.A.1    Khokhlatchev, A.2    Stippec, S.3    White, M.A.4    Cobb, M.H.5
  • 14
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42
    • Fukuoka, M., S. Suetsugu, H. Miki, K. Fukami, T. Endo, and T. Takenawa. 2001. A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42. J. Cell Biol. 152:471-482.
    • (2001) J. Cell Biol. , vol.152 , pp. 471-482
    • Fukuoka, M.1    Suetsugu, S.2    Miki, H.3    Fukami, K.4    Endo, T.5    Takenawa, T.6
  • 16
    • 0035168442 scopus 로고    scopus 로고
    • Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons
    • Herreros, J., T. Ng, and G. Schiavo. 2001. Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons. Mol. Biol. Cell 12:2947-2960.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2947-2960
    • Herreros, J.1    Ng, T.2    Schiavo, G.3
  • 17
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs, H. N., and T. D. Pollard. 2000. Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150:1311-1320.
    • (2000) J. Cell Biol. , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 18
    • 0036083157 scopus 로고    scopus 로고
    • WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation
    • Kato, M., H. Miki, S. Kurita, T. Endo, H. Nakagawa, S. Miyamoto, and T. Takenawa. 2002. WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation. Biochem. Biophys. Res Commun. 291:41-47.
    • (2002) Biochem. Biophys. Res Commun. , vol.291 , pp. 41-47
    • Kato, M.1    Miki, H.2    Kurita, S.3    Endo, T.4    Nakagawa, H.5    Miyamoto, S.6    Takenawa, T.7
  • 19
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels, M. M., and B. Qualmann. 2002. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J. 21:6083-6094.
    • (2002) EMBO J. , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 21
    • 1542373753 scopus 로고    scopus 로고
    • Coactivation of rac1 and cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor
    • Kurokawa, K., R. E. Itoh, H. Yoshizaki, Y. O. Nakamura, and M. Matsuda. 2004. Coactivation of rac1 and cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor. Mol. Biol. Cell 15:1003-1010.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1003-1010
    • Kurokawa, K.1    Itoh, R.E.2    Yoshizaki, H.3    Nakamura, Y.O.4    Matsuda, M.5
  • 22
    • 0036303142 scopus 로고    scopus 로고
    • A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility
    • Legg, J. W., C. A. Lewis, M. Parsons, T. Ng, and C. M. Isacke. 2002. A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility. Nat. Cell Biol. 27:399-401.
    • (2002) Nat. Cell Biol. , vol.27 , pp. 399-401
    • Legg, J.W.1    Lewis, C.A.2    Parsons, M.3    Ng, T.4    Isacke, C.M.5
  • 23
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel, S., S. Benesch, K. Rottner, T. Franz, J. Wehland, and R. Kuhn. 2001. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2:850-857.
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 24
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck
    • Lu, W., S. Katz, R. Gupta, and B. J. Mayer. 1997. Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol. 7:85-94.
    • (1997) Curr. Biol. , vol.7 , pp. 85-94
    • Lu, W.1    Katz, S.2    Gupta, R.3    Mayer, B.J.4
  • 27
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes
    • Manser, E., H. Y. Huang, T. H. Loo, X. Q. Chen, J. M. Dong, T. Leung, and L. Lim. 1997. Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes. Mol. Cell. Biol. 17:1129-1143.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6    Lim, L.7
  • 28
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., T. Leung, H. Salihuddin, Z. S. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367:40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 31
    • 0038375063 scopus 로고    scopus 로고
    • Inhibition of aggressiveness of metastatic mouse mammary carcinoma cells by the beta2-chimaerin GAP domain
    • Menna, P. L., G. Skilton, F. C. Leskow, D. F. Alonso, D. E. Gomez, and M. G. Kazanietz. 2003. Inhibition of aggressiveness of metastatic mouse mammary carcinoma cells by the beta2-chimaerin GAP domain. Cancer Res. 63:2284-2291.
    • (2003) Cancer Res. , vol.63 , pp. 2284-2291
    • Menna, P.L.1    Skilton, G.2    Leskow, F.C.3    Alonso, D.F.4    Gomez, D.E.5    Kazanietz, M.G.6
  • 32
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki, H., T. Sasaki, Y. Takai, and T. Takenawa. 1998. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391:93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 33
    • 0032558696 scopus 로고    scopus 로고
    • Distinct cellular effects and interactions of the Rho-family GTPase TC10
    • Neudauer, C. L., G. Joberty, N. Tatsis, and I. G. Macara. 1998. Distinct cellular effects and interactions of the Rho-family GTPase TC10. Curr. Biol. 8:1151-1160.
    • (1998) Curr. Biol. , vol.8 , pp. 1151-1160
    • Neudauer, C.L.1    Joberty, G.2    Tatsis, N.3    Macara, I.G.4
  • 35
    • 0033565261 scopus 로고    scopus 로고
    • PKCa regulates b1 integrin-dependent motility, through association and control of integrin traffic
    • Ng, T., D. Shima, A. Squire, P. I. H. Bastiaens, S. Gschmeissner, M. J. Humphries, and P. J. Parker. 1999. PKCa regulates b1 integrin-dependent motility, through association and control of integrin traffic. EMBO J. 18:3909-3923.
    • (1999) EMBO J. , vol.18 , pp. 3909-3923
    • Ng, T.1    Shima, D.2    Squire, A.3    Bastiaens, P.I.H.4    Gschmeissner, S.5    Humphries, M.J.6    Parker, P.J.7
  • 37
    • 0037458578 scopus 로고    scopus 로고
    • Neural Wiskott-Aldrich syndrome protein is recruited to rafts and associates with endophilin A in response to epidermal growth factor
    • Otsuki, M., T. Itoh, and T. Takenawa. 2003. Neural Wiskott-Aldrich syndrome protein is recruited to rafts and associates with endophilin A in response to epidermal growth factor. J. Biol. Chem. 278:6461-6469.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6461-6469
    • Otsuki, M.1    Itoh, T.2    Takenawa, T.3
  • 39
    • 0036368137 scopus 로고    scopus 로고
    • Intracellular coupling of adhesion receptors: Molecular proximity measurements
    • Parsons, M., and T. Ng. 2002. Intracellular coupling of adhesion receptors: molecular proximity measurements. Methods Cell Biol. 69:261-278.
    • (2002) Methods Cell Biol. , vol.69 , pp. 261-278
    • Parsons, M.1    Ng, T.2
  • 40
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda, K. E., J. A. Scott, R. Dyche Mullins, and W. A. Lim. 2000. Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290:801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Dyche Mullins, R.3    Lim, W.A.4
  • 41
    • 0035860812 scopus 로고    scopus 로고
    • Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1
    • Richnau, N., and P. Aspenstrom. 2001. Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J. Biol. Chem. 276:35060-35070.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35060-35070
    • Richnau, N.1    Aspenstrom, P.2
  • 42
    • 0035908956 scopus 로고    scopus 로고
    • PDGF-regulated rab4-dependent recycling of alphavbeta3 integrin from early endosomes is necessary for cell adhesion and spreading
    • Roberts, M., S. Barry, A. Woods, P. van der Sluijs, and J. Norman. 2001. PDGF-regulated rab4-dependent recycling of alphavbeta3 integrin from early endosomes is necessary for cell adhesion and spreading. Curr. Biol. 11:1392-1402.
    • (2001) Curr. Biol. , vol.11 , pp. 1392-1402
    • Roberts, M.1    Barry, S.2    Woods, A.3    Van Der Sluijs, P.4    Norman, J.5
  • 43
  • 44
    • 0034739851 scopus 로고    scopus 로고
    • Temporal and spatial distribution of activated Pak1 in fibroblasts
    • Sells, M. A., A. Pfaff, and J. Chernoff. 2000. Temporal and spatial distribution of activated Pak1 in fibroblasts. J. Cell Biol. 151:1449-1458.
    • (2000) J. Cell Biol. , vol.151 , pp. 1449-1458
    • Sells, M.A.1    Pfaff, A.2    Chernoff, J.3
  • 45
    • 0021806048 scopus 로고
    • A new method of preparing gold probes for multiple-labeling cytochemistry
    • Slot, J. W., and H. J. Geuze. 1985. A new method of preparing gold probes for multiple-labeling cytochemistry. Eur. J. Cell Biol. 38:87-93.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 47
    • 2542451854 scopus 로고    scopus 로고
    • Constitutive PAK activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions
    • Stofega, M. R., L. C. Sanders, E. M. Gardiner, and G. M. Bokoch. 2004. Constitutive PAK activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions. Mol. Biol. Cell 15:2965-2977.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2965-2977
    • Stofega, M.R.1    Sanders, L.C.2    Gardiner, E.M.3    Bokoch, G.M.4
  • 48
    • 14044260824 scopus 로고    scopus 로고
    • N-WASP deficiency reveals a role of N-WASP in the early secretory pathway
    • abstract 1760
    • Sun, H., Martinez.M., Y. Wei, S. Snapper, and H. L. Yin. 2002. N-WASP deficiency reveals a role of N-WASP in the early secretory pathway. Mol. Biol. Cell 13(Suppl.):313a (abstract 1760).
    • (2002) Mol. Biol. Cell , vol.13 , Issue.SUPPL.
    • Sun, H.1    Martinez, M.2    Wei, Y.3    Snapper, S.4    Yin, H.L.5
  • 49
    • 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
    • 0042232206 scopus 로고    scopus 로고
    • Localized cdc42 activation, detected using a novel assay, mediates microtubule organizing center positioning in endothelial cells in response to fluid shear stress
    • Tzima, E., W. B. Kiosses, M. A. del Pozo, and M. A. Schwartz. 2003. Localized cdc42 activation, detected using a novel assay, mediates microtubule organizing center positioning in endothelial cells in response to fluid shear stress. J. Biol. Chem. 278:31020-31023.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31020-31023
    • Tzima, E.1    Kiosses, W.B.2    Del Pozo, M.A.3    Schwartz, M.A.4
  • 52
    • 0034680834 scopus 로고    scopus 로고
    • Regulatable expression of p21-activated kinase-1 promotes anchorage-independent growth and abnormal organization of mitotic spindles in human epithelial breast cancer cells
    • Vadlamudi, R. K., L. Adam, R. A. Wang, M. Mandal, D. Nguyen, A. Sahin, J. Chernoff, M. C. Hung, and R. Kumar. 2000. Regulatable expression of p21-activated kinase-1 promotes anchorage-independent growth and abnormal organization of mitotic spindles in human epithelial breast cancer cells. J. Biol. Chem. 275:36238-36244.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36238-36244
    • Vadlamudi, R.K.1    Adam, L.2    Wang, R.A.3    Mandal, M.4    Nguyen, D.5    Sahin, A.6    Chernoff, J.7    Hung, M.C.8    Kumar, R.9
  • 53
    • 0037241265 scopus 로고    scopus 로고
    • Evaluation of global analysis algorithms for single frequency fluorescence lifetime imaging microscopy data
    • Verveer, P. J., and P. I. Bastiaens. 2003. Evaluation of global analysis algorithms for single frequency fluorescence lifetime imaging microscopy data. J. Microsc. 209:1-7.
    • (2003) J. Microsc. , vol.209 , pp. 1-7
    • Verveer, P.J.1    Bastiaens, P.I.2
  • 54
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer, P. J., A. Squire, and P. I. Bastiaens. 2000. Global analysis of fluorescence lifetime imaging microscopy data. Biophys. J. 78:2127-2137.
    • (2000) Biophys. J. , vol.78 , pp. 2127-2137
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.3
  • 55
    • 0034961126 scopus 로고    scopus 로고
    • Improved spatial discrimination of protein reaction states in cells by global analysis and deconvolution of fluorescence lifetime imaging microscopy data
    • Verveer, P. J., A. Squire, and P. I. Bastiaens. 2001. Improved spatial discrimination of protein reaction states in cells by global analysis and deconvolution of fluorescence lifetime imaging microscopy data. J. Microsc. 202:451-456.
    • (2001) J. Microsc. , vol.202 , pp. 451-456
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.3
  • 56
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P. J., F. S. Wouters, A. R. Reynolds, and P. I. Bastiaens. 2000. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290:1567-1570.
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 58
    • 0742305684 scopus 로고    scopus 로고
    • Visualization of spatially and temporally regulated N-WASP activity during cytoskeletal reorganization in living cells
    • Ward, M. E., J. Y. Wu, and Y. Rao. 2004. Visualization of spatially and temporally regulated N-WASP activity during cytoskeletal reorganization in living cells. Proc. Natl. Acad. Sci. USA 101:970-974.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 970-974
    • Ward, M.E.1    Wu, J.Y.2    Rao, Y.3
  • 59
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network
    • Wilcke, M., L. Johannes, T. Galli, V. Mayau, B. Goud, and J. Salamero. 2000. Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-Golgi network. J. Cell Biol. 151:1207-1220.
    • (2000) J. Cell Biol. , vol.151 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6
  • 60
    • 0038457895 scopus 로고    scopus 로고
    • Regulation of leading edge microtubule and actin dynamics downstream of Rac1
    • Wittmann, T., G. M. Bokoch, and C. M. Waterman-Storer. 2003. Regulation of leading edge microtubule and actin dynamics downstream of Rac1. J. Cell Biol. 161:845-851.
    • (2003) J. Cell Biol. , vol.161 , pp. 845-851
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3
  • 61
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke, F. T., C. C. King, B. P. Bohl, and G. M. Bokoch. 1999. Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J. Biol. Chem. 274:32565-32573.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.