메뉴 건너뛰기




Volumn 196, Issue 3, 2003, Pages 483-492

Vasopressin-induced intracellular redistribution of protein kinase D in intestinal epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GREEN FLUORESCENT PROTEIN; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE D; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; VASOPRESSIN;

EID: 0042769227     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/jcp.10323     Document Type: Article
Times cited : (22)

References (66)
  • 1
    • 0033570147 scopus 로고    scopus 로고
    • Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor
    • Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A. 1999. Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. EMBO J 18:5567-5576.
    • (1999) EMBO J , vol.18 , pp. 5567-5576
    • Bagowski, C.P.1    Stein-Gerlach, M.2    Choidas, A.3    Ullrich, A.4
  • 2
    • 0032563807 scopus 로고    scopus 로고
    • Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2
    • Ben-Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ. 1998. Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2. Curr Biol 8:1049-1057.
    • (1998) Curr Biol , vol.8 , pp. 1049-1057
    • Ben-Levy, R.1    Hooper, S.2    Wilson, R.3    Paterson, H.F.4    Marshall, C.J.5
  • 3
    • 0033527066 scopus 로고    scopus 로고
    • An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation
    • Bowden ET, Barth M, Thomas D, Glazer RI, Mueller SC. 1999. An invasion-related complex of cortactin, paxillin and PKCmu associates with invadopodia at sites of extracellular matrix degradation. Oncogene 18:4440-4449.
    • (1999) Oncogene , vol.18 , pp. 4440-4449
    • Bowden, E.T.1    Barth, M.2    Thomas, D.3    Glazer, R.I.4    Mueller, S.C.5
  • 4
    • 0035034038 scopus 로고    scopus 로고
    • Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX
    • Brownawell AM, Kops GJ, Macara IG, Burgering BM. 2001. Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. Mol Cell Biol 21:3534-3546.
    • (2001) Mol Cell Biol , vol.21 , pp. 3534-3546
    • Brownawell, A.M.1    Kops, G.J.2    Macara, I.G.3    Burgering, B.M.4
  • 5
    • 0033989653 scopus 로고    scopus 로고
    • The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus
    • Buchner K. 2000. The role of protein kinase C in the regulation of cell growth and in signalling to the cell nucleus. J Cancer Res Clin Oncol 126:1-11.
    • (2000) J Cancer Res Clin Oncol , vol.126 , pp. 1-11
    • Buchner, K.1
  • 6
    • 0032578017 scopus 로고    scopus 로고
    • Growth control mechanisms in normal and transformed intestinal cells
    • Burgess AW. 1998. Growth control mechanisms in normal and transformed intestinal cells. Philos Trans R Soc Lond B Biol Sci 353:903-909.
    • (1998) Philos Trans R Soc Lond B Biol Sci , vol.353 , pp. 903-909
    • Burgess, A.W.1
  • 7
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk- and rsk-encoded protein kinases
    • Chen RH, Sarnecki C, Blenis J. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol Cell Biol 12:915-927.
    • (1992) Mol Cell Biol , vol.12 , pp. 915-927
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 8
    • 0034996179 scopus 로고    scopus 로고
    • PKD in intestinal epithelial cells: Rapid activation by phorbol esters, LPA, and angiotensin through PKC
    • Chiu T, Rozengurt E. 2001. PKD in intestinal epithelial cells: Rapid activation by phorbol esters, LPA, and angiotensin through PKC. Am J Physiol Cell Physiol 280:C929-C942.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Chiu, T.1    Rozengurt, E.2
  • 10
    • 0035877590 scopus 로고    scopus 로고
    • Regulation of nuclear localization during signaling
    • Cyert MS. 2001. Regulation of nuclear localization during signaling. J Biol Chem 276:20805-20808.
    • (2001) J Biol Chem , vol.276 , pp. 20805-20808
    • Cyert, M.S.1
  • 11
    • 0027436376 scopus 로고
    • Cytokine modulation of intestinal epithelial cell restitution: Central role of transforming growth factor beta
    • Dignass AU, Podolsky DK. 1993. Cytokine modulation of intestinal epithelial cell restitution: Central role of transforming growth factor beta. Gastroenterology 105:1323-1332.
    • (1993) Gastroenterology , vol.105 , pp. 1323-1332
    • Dignass, A.U.1    Podolsky, D.K.2
  • 12
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod M, Ohno M, Yoshida M, Mattaj IW. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 13
    • 0030972494 scopus 로고    scopus 로고
    • Interaction of MAP kinase with MAP kinase kinase: Its possible role in the control of nucleocytoplasmic transport of MAP kinase
    • Fukuda M, Gotoh Y, Nishida E. 1997. Interaction of MAP kinase with MAP kinase kinase: Its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J 16:1901-1908.
    • (1997) EMBO J , vol.16 , pp. 1901-1908
    • Fukuda, M.1    Gotoh, Y.2    Nishida, E.3
  • 14
    • 0035827321 scopus 로고    scopus 로고
    • The rules and roles of nucleocytoplasmic shuttling proteins
    • Gama-Carvalho M, Carmo-Fonseca M. 2001. The rules and roles of nucleocytoplasmic shuttling proteins. FEBS Lett 498:157-163.
    • (2001) FEBS Lett , vol.498 , pp. 157-163
    • Gama-Carvalho, M.1    Carmo-Fonseca, M.2
  • 15
    • 0031811114 scopus 로고    scopus 로고
    • Intestinal fibroblasts regulate intestinal epithelial cell proliferation via hepatocyte growth factor
    • Goke M, Kanai M, Podolsky DK. 1998. Intestinal fibroblasts regulate intestinal epithelial cell proliferation via hepatocyte growth factor. Am J Physiol 274:G809-G818.
    • (1998) Am J Physiol , vol.274
    • Goke, M.1    Kanai, M.2    Podolsky, D.K.3
  • 16
    • 0027225936 scopus 로고
    • Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus
    • Gonzalez FA, Seth A, Raden DL, Bowman DS, Fay FS, Davis RJ. 1993. Serum-induced translocation of mitogen-activated protein kinase to the cell surface ruffling membrane and the nucleus. J Cell Biol 122: 1089-1101.
    • (1993) J Cell Biol , vol.122 , pp. 1089-1101
    • Gonzalez, F.A.1    Seth, A.2    Raden, D.L.3    Bowman, D.S.4    Fay, F.S.5    Davis, R.J.6
  • 17
    • 0037086167 scopus 로고    scopus 로고
    • Neurotensin induces protein kinase C-dependent protein kinase D activation and DNA synthesis in human pancreatic carcinoma cell line PANC-1
    • Guha S, Rey O, Rozengurt E. 2002. Neurotensin induces protein kinase C-dependent protein kinase D activation and DNA synthesis in human pancreatic carcinoma cell line PANC-1. Cancer Res 62: 1632-1640.
    • (2002) Cancer Res , vol.62 , pp. 1632-1640
    • Guha, S.1    Rey, O.2    Rozengurt, E.3
  • 18
    • 0034813992 scopus 로고    scopus 로고
    • Protein kinase D is sufficient to suppress EGF-induced c-Jun Ser 63 phosphorylation
    • Hurd C, Rozengurt E. 2001. Protein kinase D is sufficient to suppress EGF-induced c-Jun Ser 63 phosphorylation. Biochem Biophys Res Commun 282:404-408.
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 404-408
    • Hurd, C.1    Rozengurt, E.2
  • 19
    • 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 RT, Rozengurt E. 2002. Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus. Oncogene 21:2154-2160.
    • (2002) Oncogene , vol.21 , pp. 2154-2160
    • Hurd, C.1    Waldron, R.T.2    Rozengurt, E.3
  • 20
    • 0031982706 scopus 로고    scopus 로고
    • Protein kinase D activation by mutations within its pleckstrin homology domain
    • Iglesias T, Rozengurt E. 1998. Protein kinase D activation by mutations within its pleckstrin homology domain. J Biol Chem 273:410-416.
    • (1998) J Biol Chem , vol.273 , pp. 410-416
    • Iglesias, T.1    Rozengurt, E.2
  • 21
    • 0033055534 scopus 로고    scopus 로고
    • Protein kinase D activation by deletion of its cysteine-rich motifs
    • Iglesias T, Rozengurt E. 1999. Protein kinase D activation by deletion of its cysteine-rich motifs. FEBS Lett 454:53-56.
    • (1999) FEBS Lett , vol.454 , pp. 53-56
    • Iglesias, T.1    Rozengurt, E.2
  • 22
    • 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. 1998a. Dissimilar phorbol ester binding properties of the individual cysteine-rich motifs of protein kinase D. FEBS Lett 437:19-23.
    • (1998) FEBS Lett , vol.437 , pp. 19-23
    • Iglesias, T.1    Matthews, S.2    Rozengurt, E.3
  • 23
    • 0032538539 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites required for protein kinase D activation
    • Iglesias T, Waldron RT, Rozengurt E. 1998b. Identification of in vivo phosphorylation sites required for protein kinase D activation. J Biol Chem 273:27662-27667.
    • (1998) J Biol Chem , vol.273 , pp. 27662-27667
    • Iglesias, T.1    Waldron, R.T.2    Rozengurt, E.3
  • 24
    • 0029965696 scopus 로고    scopus 로고
    • Protein kinase C isozymes and substrates
    • Jaken S. 1996. Protein kinase C isozymes and substrates. Curr Opin Cell Biol 8:168-173.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 168-173
    • Jaken, S.1
  • 27
    • 0032173438 scopus 로고    scopus 로고
    • Protein kinase Cmu downregulation of tumor-necrosis-factor-induced apoptosis correlates with enhanced expression of nuclear-factor-kappaB-dependent protective genes
    • Johannes FJ, Horn J, Link G, Haas E, Siemienski K, Wajant H, Pfizenmaier K. 1998. Protein kinase Cmu downregulation of tumor-necrosis-factor-induced apoptosis correlates with enhanced expression of nuclear-factor-kappaB-dependent protective genes. Eur J Biochem 257:47-54.
    • (1998) Eur J Biochem , vol.257 , pp. 47-54
    • Johannes, F.J.1    Horn, J.2    Link, G.3    Haas, E.4    Siemienski, K.5    Wajant, H.6    Pfizenmaier, K.7
  • 28
    • 0033279823 scopus 로고    scopus 로고
    • Regulation of nuclear localization: A key to a door
    • Kaffman A, O'Shea EK. 1999. Regulation of nuclear localization: A key to a door. Ann Rev Cell Dev Biol 15:291-339.
    • (1999) Ann Rev Cell Dev Biol , vol.15 , pp. 291-339
    • Kaffman, A.1    O'Shea, E.K.2
  • 29
    • 0031915586 scopus 로고    scopus 로고
    • Intestinal trefoil factor induces inactivation of extracellular signal-regulated protein kinase in intestinal epithelial cells
    • Kanai M, Mullen C, Podolsky DK. 1998. Intestinal trefoil factor induces inactivation of extracellular signal-regulated protein kinase in intestinal epithelial cells. Proc Natl Acad Sci USA 95:178-182.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 178-182
    • Kanai, M.1    Mullen, C.2    Podolsky, D.K.3
  • 31
    • 0027283659 scopus 로고
    • Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts
    • Lenormand P, Sardet C, Pagès G, L'Allemain G, Brunet A, Pouysségur J. 1993. Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts. J Cell Biol 122:1079-1088.
    • (1993) J Cell Biol , vol.122 , pp. 1079-1088
    • Lenormand, P.1    Sardet, C.2    Pagès, G.3    L'Allemain, G.4    Brunet, A.5    Pouysségur, J.6
  • 32
  • 33
    • 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. 2001. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell 104:409-420.
    • (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
  • 34
    • 0030856559 scopus 로고    scopus 로고
    • Bryostatin 1 induces biphasic activation of protein kinase D in intact cells
    • Matthews SA, Pettit GR, Rozengurt E. 1997. Bryostatin 1 induces biphasic activation of protein kinase D in intact cells. J Biol Chem 272:20245-20250.
    • (1997) J Biol Chem , vol.272 , pp. 20245-20250
    • Matthews, S.A.1    Pettit, G.R.2    Rozengurt, E.3
  • 35
    • 0032855089 scopus 로고    scopus 로고
    • Dynamic redistribution of protein kinase D (PKD) as revealed by a GFP-PKD fusion protein: Dissociation from PKD activation
    • Matthews S, Iglesias T, Cantrell D, Rozengurt E. 1999. Dynamic redistribution of protein kinase D (PKD) as revealed by a GFP-PKD fusion protein: Dissociation from PKD activation. FEBS Lett 457: 515-521.
    • (1999) FEBS Lett , vol.457 , pp. 515-521
    • Matthews, S.1    Iglesias, T.2    Cantrell, D.3    Rozengurt, E.4
  • 36
    • 0034659737 scopus 로고    scopus 로고
    • Spatial and temporal regulation of protein kinase D (PKD)
    • Matthews SA, Iglesias T, Rozengurt E, Cantrell D. 2000. Spatial and temporal regulation of protein kinase D (PKD). EMBO J 19:2935-2945.
    • (2000) EMBO J , vol.19 , pp. 2935-2945
    • Matthews, S.A.1    Iglesias, T.2    Rozengurt, E.3    Cantrell, D.4
  • 38
    • 0030358829 scopus 로고    scopus 로고
    • Roles of the MAP kinase cascade in vertebrates
    • Moriguchi T, Gotoh Y, Nishida E. 1996. Roles of the MAP kinase cascade in vertebrates. Adv Pharmacol 36:121-137.
    • (1996) Adv Pharmacol , vol.36 , pp. 121-137
    • Moriguchi, T.1    Gotoh, Y.2    Nishida, E.3
  • 39
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton AC. 1997. Regulation of protein kinase C. Curr Opin Cell Biol 9:161-167.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 40
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari B, Bachelerie F, Dargemont C. 1997. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278:141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 41
    • 0035918217 scopus 로고    scopus 로고
    • Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C lambda
    • Perander M, Bjorkoy G, Johansen T. 2001. Nuclear import and export signals enable rapid nucleocytoplasmic shuttling of the atypical protein kinase C lambda. J Biol Chem 276:13015-13024.
    • (2001) J Biol Chem , vol.276 , pp. 13015-13024
    • Perander, M.1    Bjorkoy, G.2    Johansen, T.3
  • 43
    • 0018394382 scopus 로고
    • Epithelioid cell cultures from rat small intestine. Characterization by morphologic and immunologic criteria
    • Quaroni A, Wands J, Trelstad RL, Isselbacher KJ. 1979. Epithelioid cell cultures from rat small intestine. Characterization by morphologic and immunologic criteria. J Cell Biol 80:248-265.
    • (1979) J Cell Biol , vol.80 , pp. 248-265
    • Quaroni, A.1    Wands, J.2    Trelstad, R.L.3    Isselbacher, K.J.4
  • 44
    • 0032895918 scopus 로고    scopus 로고
    • Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells
    • Ray RM, Zimmerman BJ, McCormack SA, Patel TB, Johnson LR. 1999. Polyamine depletion arrests cell cycle and induces inhibitors p21(Waf1/Cip1), p27(Kip1), and p53 in IEC-6 cells. Am J Physiol 276:C684-C691.
    • (1999) Am J Physiol , vol.276
    • Ray, R.M.1    Zimmerman, B.J.2    McCormack, S.A.3    Patel, T.B.4    Johnson, L.R.5
  • 45
    • 0035860186 scopus 로고    scopus 로고
    • Protein kinase D interacts with Golgi via its Cysteine-rich domain
    • Rey O, Rozengurt E. 2001. Protein kinase D interacts with Golgi via its Cysteine-rich domain. Biochem Biophys Res Commun 287:21-26.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 21-26
    • Rey, O.1    Rozengurt, E.2
  • 46
    • 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. 2001a. Regulated nucleocytoplasmic transport of protein kinase D in response to G protein-coupled receptor activation. J Biol Chem 276:49228-49235.
    • (2001) J Biol Chem , vol.276 , pp. 49228-49235
    • Rey, O.1    Sinnett-Smith, J.2    Zhukova, E.3    Rozengurt, E.4
  • 47
    • 0035979991 scopus 로고    scopus 로고
    • Rapid protein kinase D translocation in response to G protein-coupled receptor activation: Dependence on protein kinase C
    • Rey O, Young SH, Cantrell D, Rozengurt E. 2001b. Rapid protein kinase D translocation in response to G protein-coupled receptor activation: Dependence on protein kinase C. J Biol Chem 276: 32616-32626.
    • (2001) J Biol Chem , vol.276 , pp. 32616-32626
    • Rey, O.1    Young, S.H.2    Cantrell, D.3    Rozengurt, E.4
  • 48
    • 0023025201 scopus 로고
    • Early signals in the mitogenic response
    • Rozengurt E. 1986. Early signals in the mitogenic response. Science 234:161-166.
    • (1986) Science , vol.234 , pp. 161-166
    • Rozengurt, E.1
  • 49
    • 0031741856 scopus 로고    scopus 로고
    • Signal transduction pathways in the mitogenic response to G protein-coupled neuropeptide receptor agonists
    • Rozengurt E. 1998. Signal transduction pathways in the mitogenic response to G protein-coupled neuropeptide receptor agonists. J Cell Physiol 177:507-517.
    • (1998) J Cell Physiol , vol.177 , pp. 507-517
    • Rozengurt, E.1
  • 50
    • 0030959013 scopus 로고    scopus 로고
    • Protein kinase D: A novel target for diacylglycerol and phorbol esters
    • Rozengurt E, Sinnett-Smith J, Zugaza JL. 1997. Protein kinase D: A novel target for diacylglycerol and phorbol esters. Biochem Soc Trans 25:565-571.
    • (1997) Biochem Soc Trans , vol.25 , pp. 565-571
    • Rozengurt, E.1    Sinnett-Smith, J.2    Zugaza, J.L.3
  • 52
    • 0029808477 scopus 로고    scopus 로고
    • Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor
    • Seufferlein T, Withers DJ, Mann D, Rozengurt E. 1996. Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor. Mol Biol Cell 7:1865-1875.
    • (1996) Mol Biol Cell , vol.7 , pp. 1865-1875
    • Seufferlein, T.1    Withers, D.J.2    Mann, D.3    Rozengurt, E.4
  • 53
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • Teruel MN, Meyer T. 2000. Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction. Cell 103:181-184.
    • (2000) Cell , vol.103 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 54
    • 0030886673 scopus 로고    scopus 로고
    • Nuclear export receptors: From importin to exportin
    • Ullman KS, Powers MA, Forbes DJ. 1997. Nuclear export receptors: From importin to exportin. Cell 90:967-970.
    • (1997) Cell , vol.90 , pp. 967-970
    • Ullman, K.S.1    Powers, M.A.2    Forbes, D.J.3
  • 55
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: A target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • Valverde AM, Sinnett-Smith J, Van Lint J, Rozengurt E. 1994. 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 91:8572-8576.
    • (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
  • 56
    • 0028881513 scopus 로고
    • Expression and characterization of PKD, a phorbol ester and diacylglycerol-stimulated serine protein kinase
    • Van Lint JV, Sinnett-Smith J, Rozengurt E. 1995. Expression and characterization of PKD, a phorbol ester and diacylglycerol-stimulated serine protein kinase. J Biol Chem 270:1455-1461.
    • (1995) J Biol Chem , vol.270 , pp. 1455-1461
    • Van Lint, J.V.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 57
    • 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
    • Waldron RT, Rozengurt E. 2003. Protein Kinase C Phosphorylates Protein Kinase D Activation Loop Ser744 and Ser748 and Releases Autoinhibition by the Pleckstrin Homology Domain. J Biol Chem 278:154-163.
    • (2003) J Biol Chem , vol.278 , pp. 154-163
    • Waldron, R.T.1    Rozengurt, E.2
  • 58
    • 0033515681 scopus 로고    scopus 로고
    • The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C
    • Waldron RT, Iglesias T, Rozengurt E. 1999. The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. J Biol Chem 274:9224-9230.
    • (1999) J Biol Chem , vol.274 , pp. 9224-9230
    • Waldron, R.T.1    Iglesias, T.2    Rozengurt, E.3
  • 59
    • 0035980125 scopus 로고    scopus 로고
    • Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo
    • Waldron R, Rey O, Iglesis T, Tugal T, Cantrell D, Rozengurt E. 2001. Activation loop Ser744 and Ser748 in protein kinase D are transphosphorylated in vivo. J Biol Chem 276:32606-32615.
    • (2001) J Biol Chem , vol.276 , pp. 32606-32615
    • Waldron, R.1    Rey, O.2    Iglesis, T.3    Tugal, T.4    Cantrell, D.5    Rozengurt, E.6
  • 60
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff B, Sanglier JJ, Wang Y. 1997. Leptomycin B is an inhibitor of nuclear export: Inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem Biol 4:139-147.
    • (1997) Chem Biol , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 62
    • 0034695691 scopus 로고    scopus 로고
    • Activation of protein kinase D by signaling through the alpha subunit of the heterotrimeric G protein G(q)
    • Yuan J, Slice L, Walsh JH, Rozengurt E. 2000. Activation of protein kinase D by signaling through the alpha subunit of the heterotrimeric G protein G(q). J Biol Chem 275:2157-2164.
    • (2000) J Biol Chem , vol.275 , pp. 2157-2164
    • Yuan, J.1    Slice, L.2    Walsh, J.H.3    Rozengurt, E.4
  • 63
    • 0012212746 scopus 로고    scopus 로고
    • Cooperation of G, Gi and G12/13 in protein kinase D activation and phosphorylation induced by lysophosphatidic acid
    • Yuan J, Slice LW, Gu J, Rozengurt E. 2002. Cooperation of Gq, Gi and G12/13 in protein kinase D activation and phosphorylation induced by lysophosphatidic acid. J Biol Chem 10:10.
    • (2002) J Biol Chem , vol.10 , pp. 10
    • Yuan, J.1    Slice, L.W.2    Gu, J.3    Rozengurt, E.4
  • 64
    • 0035955735 scopus 로고    scopus 로고
    • Protein kinase D potentiates DNA synthesis and cell proliferation induced by bombesin, vasopressin or phorbol esters in Swiss 3Te cells
    • Zhukova E, Sinnett-Smith J, Rozengurt E. 2001. Protein kinase D potentiates DNA synthesis and cell proliferation induced by bombesin, vasopressin or phorbol esters in Swiss 3Te cells. J Biol Chem 276:40298-40305.
    • (2001) J Biol Chem , vol.276 , pp. 40298-40305
    • Zhukova, E.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 65
    • 0029964752 scopus 로고    scopus 로고
    • Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway
    • Zugaza JL, Sinnett-Smith J, Van Lint J, Rozengurt E. 1996. Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway. EMBO J 15:6220-6230.
    • (1996) EMBO J , vol.15 , pp. 6220-6230
    • Zugaza, J.L.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 66
    • 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
    • Zugaza JL, Waldron RT, Sinnett-Smith J, Rozengurt E. 1997. 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 272:23952-23960.
    • (1997) J Biol Chem , vol.272 , pp. 23952-23960
    • Zugaza, J.L.1    Waldron, R.T.2    Sinnett-Smith, J.3    Rozengurt, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.