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Volumn 335, Issue 2, 2005, Pages 270-276

Protein kinase D3 activation and phosphorylation by signaling through Gαq

Author keywords

Bombesin; Diacylglycerol; G protein coupled receptor; G proteins; Neuropeptide; Phorbol esters; PKC

Indexed keywords

ALUMINUM FLUORIDE; BOMBESIN RECEPTOR; DIACYLGLYCEROL; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA Q SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; NEUROPEPTIDE; PHORBOL ESTER DERIVATIVE; PROTEIN KINASE C; PROTEIN KINASE D; PROTEIN KINASE D 3; UNCLASSIFIED DRUG;

EID: 23744501055     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.06.209     Document Type: Article
Times cited : (9)

References (42)
  • 2
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: A target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • A.M. Valverde, J. Sinnett-Smith, J. Van Lint, and E. Rozengurt Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain Proc. Natl. Acad. Sci. USA 91 1994 8572 8576
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8572-8576
    • Valverde, A.M.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 5
    • 0037592334 scopus 로고    scopus 로고
    • Protein kinase C nu/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G protein-coupled receptor agonists
    • O. Rey, J. Yuan, S.H. Young, and E. Rozengurt Protein kinase C nu/protein kinase D3 nuclear localization, catalytic activation, and intracellular redistribution in response to G protein-coupled receptor agonists J. Biol. Chem. 278 2003 23773 23785
    • (2003) J. Biol. Chem. , vol.278 , pp. 23773-23785
    • Rey, O.1    Yuan, J.2    Young, S.H.3    Rozengurt, E.4
  • 6
    • 0038339419 scopus 로고    scopus 로고
    • Genomic analysis of the eukaryotic protein kinase superfamily: A perspective
    • S.K. Hanks Genomic analysis of the eukaryotic protein kinase superfamily: a perspective Genome Biol. 4 2003 111
    • (2003) Genome Biol. , vol.4 , pp. 111
    • Hanks, S.K.1
  • 8
    • 0030771317 scopus 로고    scopus 로고
    • Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C-dependent signal transduction pathway
    • J.L. Zugaza, R.T. Waldron, J. Sinnett-Smith, and E. Rozengurt Bombesin, vasopressin, endothelin, bradykinin, and platelet-derived growth factor rapidly activate protein kinase D through a protein kinase C-dependent signal transduction pathway J. Biol. Chem. 272 1997 23952 23960
    • (1997) J. Biol. Chem. , vol.272 , pp. 23952-23960
    • Zugaza, J.L.1    Waldron, R.T.2    Sinnett-Smith, J.3    Rozengurt, E.4
  • 9
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • J.L. Zugaza, J. Sinnett-Smith, J. Van Lint, and E. Rozengurt Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway EMBO J. 15 1996 6220 6230
    • (1996) EMBO J. , vol.15 , pp. 6220-6230
    • Zugaza, J.L.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 10
    • 0034595789 scopus 로고    scopus 로고
    • Oxidative stress induces protein kinase D activation in intact cells-involvement of Src and dependence on protein kinase C
    • R.T. Waldron, and E. Rozengurt Oxidative stress induces protein kinase D activation in intact cells-involvement of Src and dependence on protein kinase C J. Biol. Chem. 275 2000 17114 17121
    • (2000) J. Biol. Chem. , vol.275 , pp. 17114-17121
    • Waldron, R.T.1    Rozengurt, E.2
  • 11
    • 0034686420 scopus 로고    scopus 로고
    • Protein kinase D. a selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes
    • S.A. Matthews, E. Rozengurt, and D. Cantrell Protein kinase D. A selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes J. Exp. Med. 191 2000 2075 2082
    • (2000) J. Exp. Med. , vol.191 , pp. 2075-2082
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3
  • 12
    • 0034996179 scopus 로고    scopus 로고
    • PKD in intestinal epithelial cells: Rapid activation by phorbol esters, LPA, and angiotensin through PKC
    • T. Chiu, and E. Rozengurt PKD in intestinal epithelial cells: rapid activation by phorbol esters, LPA, and angiotensin through PKC Am. J. Physiol. Cell Physiol. 280 2001 C929 C942
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Chiu, T.1    Rozengurt, E.2
  • 14
    • 0038136906 scopus 로고    scopus 로고
    • Cooperation of Gq, Gi, and G12/13 in protein kinase D activation and phosphorylation induced by lysophosphatidic acid
    • J. Yuan, L.W. Slice, J. Gu, and E. Rozengurt Cooperation of Gq, Gi, and G12/13 in protein kinase D activation and phosphorylation induced by lysophosphatidic acid J. Biol. Chem. 278 2003 4882 4891
    • (2003) J. Biol. Chem. , vol.278 , pp. 4882-4891
    • Yuan, J.1    Slice, L.W.2    Gu, J.3    Rozengurt, E.4
  • 15
    • 3042637596 scopus 로고    scopus 로고
    • Oxidative stress induces protein kinase C-mediated activation loop phosphorylation and nuclear redistribution of protein kinase D
    • R.T. Waldron, O. Rey, E. Zhukova, and E. Rozengurt Oxidative stress induces protein kinase C-mediated activation loop phosphorylation and nuclear redistribution of protein kinase D J. Biol. Chem. 279 2004 27482 27493
    • (2004) J. Biol. Chem. , vol.279 , pp. 27482-27493
    • Waldron, R.T.1    Rey, O.2    Zhukova, E.3    Rozengurt, E.4
  • 16
    • 0032538539 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites required for protein kinase D activation
    • T. Iglesias, R.T. Waldron, and E. Rozengurt Identification of in vivo phosphorylation sites required for protein kinase D activation J. Biol. Chem. 273 1998 27662 27667
    • (1998) J. Biol. Chem. , vol.273 , pp. 27662-27667
    • Iglesias, T.1    Waldron, R.T.2    Rozengurt, E.3
  • 17
    • 0035980125 scopus 로고    scopus 로고
    • Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo
    • R.T. Waldron, O. Rey, T. Iglesias, T. Tugal, D. Cantrell, and E. Rozengurt Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo J. Biol. Chem. 276 2001 32606 32615
    • (2001) J. Biol. Chem. , vol.276 , pp. 32606-32615
    • Waldron, R.T.1    Rey, O.2    Iglesias, T.3    Tugal, T.4    Cantrell, D.5    Rozengurt, E.6
  • 18
    • 0037414763 scopus 로고    scopus 로고
    • Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain
    • R.T. Waldron, and E. Rozengurt Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain J. Biol. Chem. 278 2003 154 163
    • (2003) J. Biol. Chem. , vol.278 , pp. 154-163
    • Waldron, R.T.1    Rozengurt, E.2
  • 19
    • 4544248747 scopus 로고    scopus 로고
    • G protein-coupled receptor-mediated phosphorylation of the activation loop of protein kinase D: Dependence on plasma membrane translocation and protein kinase Cepsilon
    • O. Rey, J.R. Reeve Jr., E. Zhukova, J. Sinnett-Smith, and E. Rozengurt G protein-coupled receptor-mediated phosphorylation of the activation loop of protein kinase D: dependence on plasma membrane translocation and protein kinase Cepsilon J. Biol. Chem. 279 2004 34361 34372
    • (2004) J. Biol. Chem. , vol.279 , pp. 34361-34372
    • Rey, O.1    Reeve Jr., J.R.2    Zhukova, E.3    Sinnett-Smith, J.4    Rozengurt, E.5
  • 20
    • 0035979991 scopus 로고    scopus 로고
    • Rapid protein kinase D translocation in response to G protein-coupled receptor activation. Dependence on protein kinase C
    • O. Rey, S.H. Young, D. Cantrell, and E. Rozengurt Rapid protein kinase D translocation in response to G protein-coupled receptor activation. Dependence on protein kinase C J. Biol. Chem. 276 2001 32616 32626
    • (2001) J. Biol. Chem. , vol.276 , pp. 32616-32626
    • Rey, O.1    Young, S.H.2    Cantrell, D.3    Rozengurt, E.4
  • 21
    • 0035955735 scopus 로고    scopus 로고
    • Protein kinase D potentiates DNA synthesis and cell proliferation induced by bombesin, vasopressin, or phorbol esters in Swiss 3T3 cells
    • E. Zhukova, J. Sinnett-Smith, and E. Rozengurt Protein kinase D potentiates DNA synthesis and cell proliferation induced by bombesin, vasopressin, or phorbol esters in Swiss 3T3 cells J. Biol. Chem. 276 2001 40298 40305
    • (2001) J. Biol. Chem. , vol.276 , pp. 40298-40305
    • Zhukova, E.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 22
    • 1942425961 scopus 로고    scopus 로고
    • Protein kinase D potentiates DNA synthesis induced by Gq-coupled receptors by increasing the duration of ERK signaling in swiss 3T3 cells
    • J. Sinnett-Smith, E. Zhukova, N. Hsieh, X. Jiang, and E. Rozengurt Protein kinase D potentiates DNA synthesis induced by Gq-coupled receptors by increasing the duration of ERK signaling in swiss 3T3 cells J. Biol. Chem. 279 2004 16883 16893
    • (2004) J. Biol. Chem. , vol.279 , pp. 16883-16893
    • Sinnett-Smith, J.1    Zhukova, E.2    Hsieh, N.3    Jiang, X.4    Rozengurt, E.5
  • 23
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • M. Liljedahl, Y. Maeda, A. Colanzi, I. Ayala, J. Van Lint, and V. Malhotra Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network Cell 104 2001 409 420
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 24
    • 0034813992 scopus 로고    scopus 로고
    • Protein kinase D is sufficient to suppress EGF-induced c-Jun Ser 63 phosphorylation
    • C. Hurd, and E. Rozengurt Protein kinase D is sufficient to suppress EGF-induced c-Jun Ser 63 phosphorylation Biochem. Biophys. Res. Commun. 282 2001 404 408
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 404-408
    • Hurd, C.1    Rozengurt, E.2
  • 25
    • 0037192716 scopus 로고    scopus 로고
    • Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus
    • C. Hurd, R.T. Waldron, and E. Rozengurt Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus Oncogene 21 2002 2154 2160
    • (2002) Oncogene , vol.21 , pp. 2154-2160
    • Hurd, C.1    Waldron, R.T.2    Rozengurt, E.3
  • 26
    • 0033570147 scopus 로고    scopus 로고
    • Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor
    • C.P. Bagowski, M. Stein-Gerlach, A. Choidas, and A. Ullrich Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor EMBO J. 18 1999 5567 5576
    • (1999) EMBO J. , vol.18 , pp. 5567-5576
    • Bagowski, C.P.1    Stein-Gerlach, M.2    Choidas, A.3    Ullrich, A.4
  • 27
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway
    • P. Storz, and A. Toker Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway EMBO J. 22 2003 109 120
    • (2003) EMBO J. , vol.22 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 28
    • 1142269809 scopus 로고    scopus 로고
    • Protein kinase D-mediated anterograde membrane trafficking is required for fibroblast motility
    • N.L. Prigozhina, and C.M. Waterman-Storer Protein kinase D-mediated anterograde membrane trafficking is required for fibroblast motility Curr. Biol. 14 2004 88 98
    • (2004) Curr. Biol. , vol.14 , pp. 88-98
    • Prigozhina, N.L.1    Waterman-Storer, C.M.2
  • 29
    • 0029855514 scopus 로고    scopus 로고
    • Organization of transmembrane signalling by heterotrimeric G proteins
    • S. Offermanns, and M.I. Simon Organization of transmembrane signalling by heterotrimeric G proteins Cancer Surv. 27 1996 177 198
    • (1996) Cancer Surv. , vol.27 , pp. 177-198
    • Offermanns, S.1    Simon, M.I.2
  • 30
    • 0027490954 scopus 로고
    • Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha
    • P.B. Wedegaertner, D.H. Chu, P.T. Wilson, M.J. Levis, and H.R. Bourne Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha J. Biol. Chem. 268 1993 25001 25008
    • (1993) J. Biol. Chem. , vol.268 , pp. 25001-25008
    • Wedegaertner, P.B.1    Chu, D.H.2    Wilson, P.T.3    Levis, M.J.4    Bourne, H.R.5
  • 31
    • 0035914392 scopus 로고    scopus 로고
    • Activation of protein kinase D by signaling through Rho and the alpha subunit of the heterotrimeric G protein G13
    • J. Yuan, L.W. Slice, and E. Rozengurt Activation of protein kinase D by signaling through Rho and the alpha subunit of the heterotrimeric G protein G13 J. Biol. Chem. 276 2001 38619 38627
    • (2001) J. Biol. Chem. , vol.276 , pp. 38619-38627
    • Yuan, J.1    Slice, L.W.2    Rozengurt, E.3
  • 32
    • 0032485940 scopus 로고    scopus 로고
    • G-alpha-12 and G-alpha-13 stimulate Rho-dependent tyrosine phosphorylation of focal adhesion kinase, paxillin, and p130 Crk-associated substrate
    • L.K. Needham, and E. Rozengurt G-alpha-12 and G-alpha-13 stimulate Rho-dependent tyrosine phosphorylation of focal adhesion kinase, paxillin, and p130 Crk-associated substrate J. Biol. Chem. 273 1998 14626 14632
    • (1998) J. Biol. Chem. , vol.273 , pp. 14626-14632
    • Needham, L.K.1    Rozengurt, E.2
  • 33
    • 0026500077 scopus 로고
    • Activation of phospholipase C by the alpha subunits of the Gq and G11 proteins in transfected Cos-7 cells
    • D.Q. Wu, C.H. Lee, S.G. Rhee, and M.I. Simon Activation of phospholipase C by the alpha subunits of the Gq and G11 proteins in transfected Cos-7 cells J. Biol. Chem. 267 1992 1811 1817
    • (1992) J. Biol. Chem. , vol.267 , pp. 1811-1817
    • Wu, D.Q.1    Lee, C.H.2    Rhee, S.G.3    Simon, M.I.4
  • 35
    • 0028931859 scopus 로고
    • Stimulation of phospholipase D by epidermal growth factor requires protein kinase C activation in Swiss 3T3 cells
    • E.J. Yeo, and J.H. Exton Stimulation of phospholipase D by epidermal growth factor requires protein kinase C activation in Swiss 3T3 cells J. Biol. Chem. 270 1995 3980 3988
    • (1995) J. Biol. Chem. , vol.270 , pp. 3980-3988
    • Yeo, E.J.1    Exton, J.H.2
  • 36
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • H.R. Bourne How receptors talk to trimeric G proteins Curr. Opin. Cell Biol. 9 1997 134 142
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 37
    • 0032562289 scopus 로고    scopus 로고
    • Targeting the receptor-Gq interface to inhibit in vivo pressure overload myocardial hypertrophy
    • S.A. Akhter, L.M. Luttrell, H.A. Rockman, G. Iaccarino, R.J. Lefkowitz, and W.J. Koch Targeting the receptor-Gq interface to inhibit in vivo pressure overload myocardial hypertrophy Science 280 1998 574 577
    • (1998) Science , vol.280 , pp. 574-577
    • Akhter, S.A.1    Luttrell, L.M.2    Rockman, H.A.3    Iaccarino, G.4    Lefkowitz, R.J.5    Koch, W.J.6
  • 38
    • 0344609797 scopus 로고    scopus 로고
    • A dominant-negative strategy for studying roles of G proteins in vivo
    • A. Gilchrist, M. Bèunemann, A. Li, M.M. Hosey, and H.E. Hamm A dominant-negative strategy for studying roles of G proteins in vivo J. Biol. Chem. 274 1999 6610 6616
    • (1999) J. Biol. Chem. , vol.274 , pp. 6610-6616
    • Gilchrist, A.1    Bèunemann, M.2    Li, A.3    Hosey, M.M.4    Hamm, H.E.5
  • 40
    • 0035952689 scopus 로고    scopus 로고
    • Transforming G proteins
    • V. Radhika, and N. Dhanasekaran Transforming G proteins Oncogene 20 2001 1607 1614
    • (2001) Oncogene , vol.20 , pp. 1607-1614
    • Radhika, V.1    Dhanasekaran, N.2
  • 42
    • 14644414790 scopus 로고    scopus 로고
    • Protein kinase cascades in the regulation of cardiac hypertrophy
    • G.W. Dorn II, and T. Force Protein kinase cascades in the regulation of cardiac hypertrophy J. Clin. Invest. 115 2005 527 537
    • (2005) J. Clin. Invest. , vol.115 , pp. 527-537
    • Dorn II, G.W.1    Force, T.2


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