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Volumn 4, Issue 4, 2003, Pages 561-574

Mechanism of persistent protein kinase D1 translocation and activation

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE D1; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG;

EID: 0037389225     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1534-5807(03)00087-X     Document Type: Article
Times cited : (52)

References (34)
  • 1
    • 0032561324 scopus 로고    scopus 로고
    • 2+ -independent protein kinase C (ηPKC) activation and its regulation by calcineurin activation
    • 2+ -independent protein kinase C (ηPKC) activation and its regulation by calcineurin activation J. Biol. Chem. 273 1998 28392 28398
    • (1998) J. Biol. Chem. , vol.273 , pp. 28392-28398
    • Asada, A.1    Zhao, Y.2    Kondo, S.3    Iwata, M.4
  • 2
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron C.L. Malhotra V. Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane Science 295 2002 325 328
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 3
    • 0030825340 scopus 로고    scopus 로고
    • Association of the G protein αq/α11-subunit with cytoskeleton in adrenal glomerulosa cells: Role in receptor-effector coupling
    • Cote M. Payet M.D. Dufour M.N. Guillon G. Gallo-Payet N. Association of the G protein αq/α11-subunit with cytoskeleton in adrenal glomerulosa cells: role in receptor-effector coupling Endocrinology 138 1997 3299 3307
    • (1997) Endocrinology , vol.138 , pp. 3299-3307
    • Cote, M.1    Payet, M.D.2    Dufour, M.N.3    Guillon, G.4    Gallo-Payet, N.5
  • 4
    • 0034674678 scopus 로고    scopus 로고
    • Proteolytic cleavage and activation of protein kinase Cμ by caspase-3 in the apoptotic response of cells to 1-β-D-arabinofuranosylcytosine and other genotoxic agents
    • Endo K. Oki E. Biedermann V. Kojima H. Yoshida K. Johannes F.J. Kufe D. Datta R. Proteolytic cleavage and activation of protein kinase Cμ by caspase-3 in the apoptotic response of cells to 1-β-D-arabinofuranosylcytosine and other genotoxic agents J. Biol. Chem. 275 2000 18476 18481
    • (2000) J. Biol. Chem. , vol.275 , pp. 18476-18481
    • Endo, K.1    Oki, E.2    Biedermann, V.3    Kojima, H.4    Yoshida, K.5    Johannes, F.J.6    Kufe, D.7    Datta, R.8
  • 5
    • 0035830890 scopus 로고    scopus 로고
    • Visualization of a functional Gαq-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not by activation mediated by receptors or AlF4
    • Hughes T.E. Zhang H. Logothetis D.E. Berlot C.H. Visualization of a functional Gαq-green fluorescent protein fusion in living cells. Association with the plasma membrane is disrupted by mutational activation and by elimination of palmitoylation sites, but not by activation mediated by receptors or AlF4 J. Biol. Chem. 276 2001 4227 4235
    • (2001) J. Biol. Chem. , vol.276 , pp. 4227-4235
    • Hughes, T.E.1    Zhang, H.2    Logothetis, D.E.3    Berlot, C.H.4
  • 6
    • 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
    • Hurd C. Waldron R.T. Rozengurt E. 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
  • 9
    • 0032538616 scopus 로고    scopus 로고
    • Dissimilar phorbol ester binding properties of the individual cysteine-rich motifs of protein kinase D
    • Iglesias T. Matthews S. Rozengurt E. Dissimilar phorbol ester binding properties of the individual cysteine-rich motifs of protein kinase D FEBS Lett. 437 1998 19 23
    • (1998) FEBS Lett. , vol.437 , pp. 19-23
    • Iglesias, T.1    Matthews, S.2    Rozengurt, E.3
  • 10
    • 0031982706 scopus 로고    scopus 로고
    • Protein kinase D activation by mutations within its pleckstrin homology domain
    • Iglesias T. Rozengurt E. Protein kinase D activation by mutations within its pleckstrin homology domain J. Biol. Chem. 273 1998 410 416
    • (1998) J. Biol. Chem. , vol.273 , pp. 410-416
    • Iglesias, T.1    Rozengurt, E.2
  • 13
    • 0037138405 scopus 로고    scopus 로고
    • Pleckstrin homology domains and the cytoskeleton
    • Lemmon M.A. Ferguson K.M. Abrams C.S. Pleckstrin homology domains and the cytoskeleton FEBS Lett. 513 2002 71 76
    • (2002) FEBS Lett. , vol.513 , pp. 71-76
    • Lemmon, M.A.1    Ferguson, K.M.2    Abrams, C.S.3
  • 14
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl M. Maeda Y. Colanzi A. Ayala I. Van Lint J. Malhotra V. 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
  • 15
    • 0026770104 scopus 로고
    • Crosstalk among multiple signal-activated phospholipases
    • Liscovitch M. Crosstalk among multiple signal-activated phospholipases Trends Biochem. Sci. 17 1992 393 399
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 393-399
    • Liscovitch, M.1
  • 16
    • 0035503293 scopus 로고    scopus 로고
    • Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
    • Maeda Y. Beznoussenko G.V. Van Lint J. Mironov A.A. Malhotra V. Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain EMBO J. 20 2001 5982 5990
    • (2001) EMBO J. , vol.20 , pp. 5982-5990
    • Maeda, Y.1    Beznoussenko, G.V.2    Van Lint, J.3    Mironov, A.A.4    Malhotra, V.5
  • 17
    • 0034659737 scopus 로고    scopus 로고
    • Spatial and temporal regulation of protein kinase D (PKD)
    • Matthews S.A. Iglesias T. Rozengurt E. Cantrell D. Spatial and temporal regulation of protein kinase D (PKD) EMBO J. 19 2000 2935 2945
    • (2000) EMBO J. , vol.19 , pp. 2935-2945
    • Matthews, S.A.1    Iglesias, T.2    Rozengurt, E.3    Cantrell, D.4
  • 18
    • 0033543570 scopus 로고    scopus 로고
    • Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cμ
    • Matthews S.A. Rozengurt E. Cantrell D. Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cμ J. Biol. Chem. 274 1999 26543 26549
    • (1999) J. Biol. Chem. , vol.274 , pp. 26543-26549
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3
  • 19
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea E. Meyer T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals Cell 95 1998 307 318
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 20
    • 0032498538 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea E. Teruel M.N. Quest A.F. Meyer T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells J. Cell Biol. 140 1998 485 498
    • (1998) J. Cell Biol. , vol.140 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.3    Meyer, T.4
  • 21
    • 0026336497 scopus 로고
    • Domain interactions in protein kinase C
    • Pears C.J. Parker P.J. Domain interactions in protein kinase C J. Cell Sci. 100 1991 683 686
    • (1991) J. Cell Sci. , vol.100 , pp. 683-686
    • Pears, C.J.1    Parker, P.J.2
  • 22
    • 0023773004 scopus 로고
    • Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes
    • Peralta E.G. Ashkenazi A. Winslow J.W. Ramachandran J. Capon D.J. Differential regulation of PI hydrolysis and adenylyl cyclase by muscarinic receptor subtypes Nature 334 1988 434 437
    • (1988) Nature , vol.334 , pp. 434-437
    • Peralta, E.G.1    Ashkenazi, A.2    Winslow, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 23
    • 0027335583 scopus 로고
    • Epitope-tagged Gq α subunits: Expression of GTPase-deficient alpha subunits persistently stimulates phosphatidylinositol-specific phospholipase C but not mitogen-activated protein kinase activity regulated by the M1 muscarinic acetylcholine receptor
    • Qian N.X. Winitz S. Johnson G.L. Epitope-tagged Gq α subunits: expression of GTPase-deficient alpha subunits persistently stimulates phosphatidylinositol-specific hospholipase C but not mitogen-activated protein kinase activity regulated by the M1 muscarinic acetylcholine receptor Proc. Natl. Acad. Sci. USA 90 1993 4077 4081
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4077-4081
    • Qian, N.X.1    Winitz, S.2    Johnson, G.L.3
  • 24
    • 0035860186 scopus 로고    scopus 로고
    • Protein kinase D interacts with Golgi via its cysteine-rich domain
    • Rey O. Rozengurt E. Protein kinase D interacts with Golgi via its cysteine-rich domain Biochem. Biophys. Res. Commun. 287 2001 21 26
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 21-26
    • Rey, O.1    Rozengurt, E.2
  • 25
    • 0035966065 scopus 로고    scopus 로고
    • Regulated nucleocytoplasmic transport of protein kinase D in response to G protein-coupled receptor activation
    • Rey O. Sinnett-Smith J. Zhukova E. Rozengurt E. Regulated nucleocytoplasmic transport of protein kinase D in response to G protein-coupled receptor activation J. Biol. Chem. 276 2001 49228 49235
    • (2001) J. Biol. Chem. , vol.276 , pp. 49228-49235
    • Rey, O.1    Sinnett-Smith, J.2    Zhukova, E.3    Rozengurt, E.4
  • 26
    • 0035051978 scopus 로고    scopus 로고
    • TRPC1 and TRPC5 form a novel cation channel in mammalian brain
    • Strubing C. Krapivinsky G. Krapivinsky L. Clapham D.E. TRPC1 and TRPC5 form a novel cation channel in mammalian brain Neuron 29 2001 645 655
    • (2001) Neuron , vol.29 , pp. 645-655
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 27
    • 0030763336 scopus 로고    scopus 로고
    • Electroporation-induced formation of individual calcium entry sites in the cell body and processes of adherent cells
    • Teruel M.N. Meyer T. Electroporation-induced formation of individual calcium entry sites in the cell body and processes of adherent cells Biophys. J. 73 1997 1785 1796
    • (1997) Biophys. J. , vol.73 , pp. 1785-1796
    • Teruel, M.N.1    Meyer, T.2
  • 28
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: A target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • Valverde A.M. Sinnett-Smith J. Van Lint J. Rozengurt E. 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
  • 29
    • 0033515681 scopus 로고    scopus 로고
    • The pleckstrin homology domain of protein kinase D interacts preferentially with the η isoform of protein kinase C
    • Waldron R.T. Iglesias T. Rozengurt E. The pleckstrin homology domain of protein kinase D interacts preferentially with the η isoform of protein kinase C J. Biol. Chem. 274 1999 9224 9230
    • (1999) J. Biol. Chem. , vol.274 , pp. 9224-9230
    • Waldron, R.T.1    Iglesias, T.2    Rozengurt, E.3
  • 30
    • 0035980125 scopus 로고    scopus 로고
    • Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo
    • Waldron R.T. Rey O. Iglesias T. Tugal T. Cantrell D. Rozengurt E. 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
  • 31
    • 0027490954 scopus 로고
    • Palmitoylation is required for signaling functions and membrane attachment of Gq α and Gs α
    • Wedegaertner P.B. Chu D.H. Wilson P.T. Levis M.J. Bourne H.R. Palmitoylation is required for signaling functions and membrane attachment of Gq α and Gs α 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
  • 33
    • 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
    • Zhukova E. Sinnett-Smith J. Rozengurt E. 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
  • 34
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • Zugaza J.L. Sinnett-Smith J. Van Lint J. Rozengurt E. 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


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