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Volumn 287, Issue 41, 2012, Pages 34604-34613

GIT1 Phosphorylation on Serine 46 by PKD3 regulates paxillin trafficking and cellular protrusive activity

Author keywords

[No Author keywords available]

Indexed keywords

CELL SPREADING; CYTOSKELETAL; DYNAMIC LOCALIZATION; FOCAL ADHESIONS; G PROTEIN COUPLED RECEPTORS; MOLECULAR SWITCHES; MULTIDOMAIN PROTEINS; PAXILLIN; PROTEIN KINASE; SUBCELLULAR LOCALIZATIONS;

EID: 84867255646     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.374652     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 41549102357 scopus 로고    scopus 로고
    • The PIX-GIT complex: A G protein signaling cassette in control of cell shape
    • Frank, S. R., and Hansen, S. H. (2008) The PIX-GIT complex: a G protein signaling cassette in control of cell shape. Semin Cell Dev. Biol. 19, 234-244
    • (2008) Semin Cell Dev. Biol. , vol.19 , pp. 234-244
    • Frank, S.R.1    Hansen, S.H.2
  • 2
    • 35148814898 scopus 로고    scopus 로고
    • Arf GAPs as regulators of the actin cytoskeleton
    • DOI 10.1042/BC20070034
    • Randazzo, P. A., Inoue, H., and Bharti, S. (2007) Arf GAPs as regulators of the actin cytoskeleton. Biol. Cell 99, 583-600 (Pubitemid 47543316)
    • (2007) Biology of the Cell , vol.99 , Issue.10 , pp. 583-600
    • Randazzo, P.A.1    Inoue, H.2    Bharti, S.3
  • 3
    • 33646705915 scopus 로고    scopus 로고
    • The multifunctional GIT family of proteins
    • DOI 10.1242/jcs.02925
    • Hoefen, R. J., and Berk, B. C. (2006) The multifunctional GIT family of proteins. J. Cell Sci. 119, 1469-1475 (Pubitemid 43732975)
    • (2006) Journal of Cell Science , vol.119 , Issue.8 , pp. 1469-1475
    • Hoefen, R.J.1    Berk, B.C.2
  • 4
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin, N. O., and Turner, C. E. (2008) Paxillin comes of age. J. Cell Sci. 121, 2435-2444
    • (2008) J. Cell Sci. , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 5
    • 0035833251 scopus 로고    scopus 로고
    • The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    • DOI 10.1083/jcb.200101039
    • West, K. A., Zhang, H., Brown, M. C., Nikolopoulos, S. N., Riedy, M. C., Horwitz, A. F., and Turner, C. E. (2001) The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). J. Cell Biol. 154, 161-176 (Pubitemid 34289286)
    • (2001) Journal of Cell Biology , vol.154 , Issue.1 , pp. 161-176
    • West, K.A.1    Zhang, H.2    Brown, M.L.C.3    Nikolopoulos, S.N.4    Riedy, M.C.5    Horwitz, A.F.6    Turner, C.E.7
  • 6
    • 17344366888 scopus 로고    scopus 로고
    • 4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells
    • DOI 10.1038/ncb1234
    • Nishiya, N., Kiosses, W. B., Han, J., and Ginsberg, M. H. (2005) An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells. Nat. Cell Biol. 7, 343-352 (Pubitemid 40533123)
    • (2005) Nature Cell Biology , vol.7 , Issue.4 , pp. 343-352
    • Nishiya, N.1    Kiosses, W.B.2    Han, J.3    Ginsberg, M.H.4
  • 7
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • DOI 10.1152/physrev.00002.2004
    • Brown, M. C., and Turner, C. E. (2004) Paxillin: adapting to change. Physiol. Rev. 84, 1315-1339 (Pubitemid 39287952)
    • (2004) Physiological Reviews , vol.84 , Issue.4 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 9
    • 0033843129 scopus 로고    scopus 로고
    • Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly
    • DOI 10.1128/MCB.20.17.6354-6363.2000
    • Zhao, Z. S., Manser, E., Loo, T. H., and Lim, L. (2000) Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly. Mol. Cell. Biol. 20, 6354-6363 (Pubitemid 30650222)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.17 , pp. 6354-6363
    • Zhao, Z.-S.1    Manser, E.2    Loo, T.-H.3    Lim, L.4
  • 10
    • 0036537895 scopus 로고    scopus 로고
    • GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration
    • Manabe, R., Kovalenko, M., Webb, D. J., and Horwitz, A. R. (2002) GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration. J. Cell Sci. 115, 1497-1510 (Pubitemid 34428707)
    • (2002) Journal of Cell Science , vol.115 , Issue.7 , pp. 1497-1510
    • Manabe, R.-I.1    Kovalenko, M.2    Webbs, D.J.3    Horwitz, A.R.4
  • 11
    • 1942518365 scopus 로고    scopus 로고
    • GIT1 Activates p21-Activated Kinase through a Mechanism Independent of p21 Binding
    • DOI 10.1128/MCB.24.9.3849-3859.2004
    • Loo, T. H., Ng, Y. W., Lim, L., and Manser, E. (2004) GIT1 activates p21-activated kinase through a mechanism independent of p21 binding. Mol. Cell Biol. 24, 3849-3859 (Pubitemid 38496163)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.9 , pp. 3849-3859
    • Loo, T.-H.1    Ng, Y.-W.2    Lim, L.3    Manser, E.4
  • 12
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway
    • DOI 10.1091/mbc.02-02-0015
    • Brown, M. C., West, K. A., and Turner, C. E. (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 (Pubitemid 34522638)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.5 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 14
    • 0035694169 scopus 로고    scopus 로고
    • Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface
    • Matafora, V., Paris, S., Dariozzi, S., and de Curtis, I. (2001) Molecular mechanisms regulating the subcellular localization of p95-APP1 between the endosomal recycling compartment and sites of actin organization at the cell surface. J. Cell Sci. 114, 4509-4520 (Pubitemid 34082871)
    • (2001) Journal of Cell Science , vol.114 , Issue.24 , pp. 4509-4520
    • Matafora, V.1    Paris, S.2    Dariozzi, S.3    De Curtis, I.4
  • 15
    • 0037738555 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1B-mediated neurite outgrowth
    • DOI 10.1091/mbc.E02-07-0406
    • Albertinazzi, C., Za, L., Paris, S., and de Curtis, I. (2003) ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1B-mediated neurite outgrowth. Mol. Biol. Cell 14, 1295-1307 (Pubitemid 36547401)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.4 , pp. 1295-1307
    • Albertinazzi, C.1    Za, L.2    Paris, S.3    De Curtis, I.4
  • 17
    • 84862811320 scopus 로고    scopus 로고
    • Phosphorylation of GIT1 tyrosine 321 is required for association with FAK at focal adhesions and for PDGF-activated migration of osteoblasts
    • Ren, Y., Yu, L., Fan, J., Rui, Z., Hua, Z., Zhang, Z., Zhang, N., and Yin, G. (2012) Phosphorylation of GIT1 tyrosine 321 is required for association with FAK at focal adhesions and for PDGF-activated migration of osteoblasts. Mol Cell Biochem. 365, 109-118
    • (2012) Mol Cell Biochem. , vol.365 , pp. 109-118
    • Ren, Y.1    Yu, L.2    Fan, J.3    Rui, Z.4    Hua, Z.5    Zhang, Z.6    Zhang, N.7    Yin, G.8
  • 18
    • 33745333951 scopus 로고    scopus 로고
    • Phosphorylation of serine 709 in GIT1 regulates protrusive activity in cells
    • DOI 10.1016/j.bbrc.2006.06.036, PII S0006291X06013416
    • Webb, D. J., Kovalenko, M., Whitmore, L., and Horwitz, A. F. (2006) Phosphorylation of serine 709 in GIT1 regulates protrusive activity in cells. Biochem. Biophys. Res. Commun. 346, 1284-1288 (Pubitemid 43946831)
    • (2006) Biochemical and Biophysical Research Communications , vol.346 , Issue.4 , pp. 1284-1288
    • Webb, D.J.1    Kovalenko, M.2    Whitmore, L.3    Horwitz, A.F.4
  • 19
    • 79961026124 scopus 로고    scopus 로고
    • Protein kinase D: Coupling extracellular stimuli to the regulation of cell physiology
    • Fu, Y., and Rubin, C. S. (2011) Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology. EMBO Rep. 12, 785-796
    • (2011) EMBO Rep. , vol.12 , pp. 785-796
    • Fu, Y.D.1    Rubin, C.S.2
  • 20
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • Wang, Q. J. (2006) PKD at the crossroads of DAG and PKC signaling. Trends Pharmacol. Sci. 27, 317-323
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 317-323
    • Wang, Q.J.1
  • 21
    • 67349096401 scopus 로고    scopus 로고
    • Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot
    • Eiseler, T., Döppler, H., Yan, I. K., Kitatani, K., Mizuno, K., and Storz, P. (2009) Protein kinase D1 regulates cofilin-mediated F-actin reorganization and cell motility through slingshot. Nat. Cell Biol. 11, 545-556
    • (2009) Nat. Cell Biol. , vol.11 , pp. 545-556
    • Eiseler, T.1    Döppler, H.2    Yan, I.K.3    Kitatani, K.4    Mizuno, K.5    Storz, P.6
  • 23
    • 79952321053 scopus 로고    scopus 로고
    • A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration
    • Ziegler, S., Eiseler, T., Scholz, R. P., Beck, A., Link, G., and Hausser, A. (2011) A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration. Mol. Biol. Cell 22, 570-580
    • (2011) Mol. Biol. Cell , vol.22 , pp. 570-580
    • Ziegler, S.1    Eiseler, T.2    Scholz, R.P.3    Beck, A.4    Link, G.5    Hausser, A.6
  • 24
    • 77953315696 scopus 로고    scopus 로고
    • Protein kinase D controls actin polymerization and cell motility through phosphorylation of cortactin
    • Eiseler, T., Hausser, A., De Kimpe, L., Van Lint, J., and Pfizenmaier, K. (2010) Protein kinase D controls actin polymerization and cell motility through phosphorylation of cortactin. J. Biol. Chem. 285, 18672-18683
    • (2010) J. Biol. Chem. , vol.285 , pp. 18672-18683
    • Eiseler, T.1    Hausser, A.2    De Kimpe, L.3    Van Lint, J.4    Pfizenmaier, K.5
  • 25
    • 67651005347 scopus 로고    scopus 로고
    • Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like
    • Peterburs, P., Heering, J., Link, G., Pfizenmaier, K., Olayioye, M. A., and Hausser, A. (2009) Protein kinase D regulates cell migration by direct phosphorylation of the cofilin phosphatase slingshot 1 like. Cancer Res. 69, 5634-5638
    • (2009) Cancer Res. , vol.69 , pp. 5634-5638
    • Peterburs, P.1    Heering, J.2    Link, G.3    Pfizenmaier, K.4    Olayioye, M.A.5    Hausser, A.6
  • 26
    • 80053195284 scopus 로고    scopus 로고
    • Protein kinase D regulates cofilin activity through p21-activated kinase 4
    • Spratley, S. J., Bastea, L. I., Döppler, H., Mizuno, K., and Storz, P. (2011) Protein kinase D regulates cofilin activity through p21-activated kinase 4. J. Biol. Chem. 286, 34254-34261
    • (2011) J. Biol. Chem. , vol.286 , pp. 34254-34261
    • Spratley, S.J.1    Bastea, L.I.2    Döppler, H.3    Mizuno, K.4    Storz, P.5
  • 27
    • 33748307404 scopus 로고    scopus 로고
    • Identification of protein networks associated with the PAK1-betaPIX-GIT1- paxillin signaling complex by mass spectrometry
    • DOI 10.1021/pr060140t
    • Mayhew, M. W., Webb, D. J., Kovalenko, M., Whitmore, L., Fox, J. W., and Horwitz, A. F. (2006) Identification of protein networks associated with the PAK1-betaPIX-GIT1-paxillin signaling complex by mass spectrometry. J. Proteome Res. 5, 2417-2423 (Pubitemid 44330835)
    • (2006) Journal of Proteome Research , vol.5 , Issue.9 , pp. 2417-2423
    • Mayhew, M.W.1    Webb, D.J.2    Kovalenko, M.3    Whitmore, L.4    Fox, J.W.5    Horwitz, A.F.6
  • 29
    • 62349122241 scopus 로고    scopus 로고
    • High accuracy mass spectrometry in large-scale analysis of protein phosphorylation
    • Olsen, J. V., and Macek, B. (2009) High accuracy mass spectrometry in large-scale analysis of protein phosphorylation. Methods Mol. Biol. 492, 131-142
    • (2009) Methods Mol. Biol. , vol.492 , pp. 131-142
    • Olsen, J.V.1    Macek, B.2
  • 30
    • 79959558401 scopus 로고    scopus 로고
    • Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast
    • Koch, A., Krug, K., Pengelley, S., Macek, B., and Hauf, S. (2011) Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast. Sci. Signal 4, rs6
    • (2011) Sci. Signal , vol.4
    • Koch, A.1    Krug, K.2    Pengelley, S.3    Macek, B.4    Hauf, S.5
  • 31
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J., Matic, I., Hilger, M., Nagaraj, N., Selbach, M., Olsen, J. V., and Mann, M. (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 32
    • 17644370387 scopus 로고    scopus 로고
    • A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D
    • DOI 10.1074/jbc.C400575200
    • Döppler, H., Storz, P., Li, J., Comb, M. J., and Toker, A. (2005) A phosphorylation state-specific antibody recognizes Hsp27, a novel substrate of protein kinase D. J. Biol. Chem. 280, 15013-15019 (Pubitemid 40562854)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15013-15019
    • Doppler, H.1    Storz, P.2    Li, J.3    Comb, M.J.4    Toker, A.5
  • 33
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • DOI 10.1083/jcb.200612017
    • Fugmann, T., Hausser, A., Schöffler, P., Schmid, S., Pfizenmaier, K., and Olayioye, M. A. (2007) Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J. Cell Biol. 178, 15-22 (Pubitemid 47026398)
    • (2007) Journal of Cell Biology , vol.178 , Issue.1 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schoffler, P.3    Schmid, S.4    Pfizenmaier, K.5    Olayioye, M.A.6
  • 34
    • 33847035916 scopus 로고    scopus 로고
    • Protein kinase D 3 is localized in vesicular structures and interacts with vesicle-associated membrane protein 2
    • DOI 10.1016/j.cellsig.2006.10.012, PII S0898656806002919
    • Lu, G., Chen, J., Espinoza, L. A., Garfield, S., Toshiyuki, S., Akiko, H., Huppler, A., and Wang, Q. J. (2007) Protein kinase D 3 is localized in vesicular structures and interacts with vesicle-associated membrane protein 2. Cell Signal 19, 867-879 (Pubitemid 46275376)
    • (2007) Cellular Signalling , vol.19 , Issue.4 , pp. 867-879
    • Lu, G.1    Chen, J.2    Espinoza, L.A.3    Garfield, S.4    Toshiyuki, S.5    Akiko, H.6    Huppler, A.7    Wang, Q.J.8
  • 35
    • 11244310645 scopus 로고    scopus 로고
    • Protein kinase C-independent effects of protein kinase D3 in glucose transport in L6 myotubes
    • DOI 10.1124/mol.104.004200
    • Chen, J., Lu, G., and Wang, Q. J. (2005) Protein kinase C-independent effects of protein kinase D3 in glucose transport in L6 myotubes. Mol. Pharmacol. 67, 152-162 (Pubitemid 40069975)
    • (2005) Molecular Pharmacology , vol.67 , Issue.1 , pp. 152-162
    • Chen, J.1    Lu, G.2    Wang, Q.J.3
  • 36
    • 45149095520 scopus 로고    scopus 로고
    • Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: Differential regulation of activation loop Ser(744) and Ser(748) phosphorylation
    • Jacamo, R., Sinnett-Smith, J., Rey, O., Waldron, R. T., and Rozengurt, E. (2008) Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: differential regulation of activation loop Ser(744) and Ser(748) phosphorylation. J. Biol. Chem. 283, 12877-12887
    • (2008) J. Biol. Chem. , vol.283 , pp. 12877-12887
    • Jacamo, R.1    Sinnett-Smith, J.2    Rey, O.3    Waldron, R.T.4    Rozengurt, E.5
  • 37
    • 34548133221 scopus 로고    scopus 로고
    • PKD is recruited to sites of actin remodelling at the leading edge and negatively regulates cell migration
    • DOI 10.1016/j.febslet.2007.07.079, PII S0014579307008605
    • Eiseler, T., Schmid, M. A., Topbas, F., Pfizenmaier, K., and Hausser, A. (2007) PKD is recruited to sites of actin remodeling at the leading edge and negatively regulates cell migration. FEBS Lett. 581, 4279-4287 (Pubitemid 47301866)
    • (2007) FEBS Letters , vol.581 , Issue.22 , pp. 4279-4287
    • Eiseler, T.1    Schmid, M.A.2    Topbas, F.3    Pfizenmaier, K.4    Hausser, A.5
  • 38
    • 67549112510 scopus 로고    scopus 로고
    • Protein kinase D1 regulates matrix metalloproteinase expression and inhibits breast cancer cell invasion
    • Eiseler, T., Döppler, H., Yan, I. K., Goodison, S., and Storz, P. (2009) Protein kinase D1 regulates matrix metalloproteinase expression and inhibits breast cancer cell invasion. Breast Cancer Res. 11, R13
    • (2009) Breast Cancer Res. , vol.11
    • Eiseler, T.1    Döppler, H.2    Yan, I.K.3    Goodison, S.4    Storz, P.5
  • 39
    • 45549091994 scopus 로고    scopus 로고
    • Protein kinase D3 (PKD3) contributes to prostate cancer cell growth and survival through a PKCε/PKD3 pathway downstream of Akt and ERK 1/2
    • Chen, J., Deng, F., Singh, S. V., and Wang, Q. J. (2008) Protein kinase D3 (PKD3) contributes to prostate cancer cell growth and survival through a PKCε/PKD3 pathway downstream of Akt and ERK 1/2. Cancer Res. 68, 3844-3853
    • (2008) Cancer Res. , vol.68 , pp. 3844-3853
    • Chen, J.1    Deng, F.2    Singh, S.V.3    Wang, Q.J.4
  • 40
    • 44049103630 scopus 로고    scopus 로고
    • Expression patterns of protein kinaseD3 during mouse development
    • Ellwanger, K., Pfizenmaier, K., Lutz, S., and Hausser, A. (2008) Expression patterns of protein kinaseD3 during mouse development. BMCDev. Biol. 8, 47
    • (2008) BMCDev. Biol. , vol.8 , pp. 47
    • Ellwanger, K.1    Pfizenmaier, K.2    Lutz, S.3    Hausser, A.4


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