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(Received for publication, March 21, 1997, and in revised form, June 16, 1997)
From the Growth Regulation Laboratory, Imperial Cancer Research
Fund, P.O. Box 123, 44 Lincoln's Inn Fields,
London WC2A 3PX, United Kingdom
Protein kinase D (PKD) is a serine/threonine
protein kinase that is activated by phorbol esters via protein kinase C
in intact cells. To assess the physiological significance of this
putative pathway, we examined the regulation of PKD in living cells by mitogenic regulatory peptides and by platelet-derived growth factors (PDGF). Our results demonstrate that bombesin rapidly induces PKD
activation in Swiss 3T3 cells, as shown by autophosphorylation and
syntide-2 phosphorylation assays. Maximum PKD activation (14-fold above
base-line levels) was obtained 90 s after bombesin stimulation. Bombesin also induced PKD activation in Rat-1 cells stably transfected with the bombesin/gastrin releasing peptide (GRP) receptor and in COS-7
cells transiently co-transfected with PKD and bombesin/GRP receptor
expression constructs. No inducible kinase activity was demonstrated
when COS-7 cells were transfected with a kinase-deficient PKD mutant.
Bombesin-mediated PKD activation was prevented by treatment of Swiss
3T3 cells with the protein kinase C inhibitors GF 1092030X and Ro
31-8220. In contrast, these compounds did not inhibit PKD activity when
added directly in vitro. Vasopressin, endothelin, and
bradykinin also activated PKD in Swiss 3T3 cells through a
PKC-dependent pathway. Platelet-derived growth
factor-stimulated PKD activation in Swiss 3T3 cells and in porcine
aortic endothelial cells stably transfected with PDGF-
Volume 272, Number 38,
Issue of September 19, 1997
pp. 23952-23960
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
receptors.
Treatment with GF 1092030X or Ro 31-8220 inhibited PKD activation
induced by PDGF. Thus, our results indicate that PKD is activated by
multiple signaling peptides through a protein kinase
C-dependent signal transduction pathway in a variety of
cell types.
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L. Paolucci, J. Sinnett-Smith, and E. Rozengurt Lysophosphatidic acid rapidly induces protein kinase D activation through a pertussis toxin-sensitive pathway Am J Physiol Cell Physiol, January 1, 2000; 278(1): C33 - C39. [Abstract] [Full Text] [PDF]
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R. S. Haworth, J. Sinnett-Smith, E. Rozengurt, and M. Avkiran Protein kinase D inhibits plasma membrane Na+/H+ exchanger activity Am J Physiol Cell Physiol, December 1, 1999; 277(6): C1202 - C1209. [Abstract] [Full Text] [PDF]
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S. A. Matthews, E. Rozengurt, and D. Cantrell Characterization of Serine 916 as an in Vivo Autophosphorylation Site for Protein Kinase D/Protein Kinase C{micro} J. Biol. Chem., September 10, 1999; 274(37): 26543 - 26549. [Abstract] [Full Text] [PDF]
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E. D. W. Moore, M. Ring, D. R. L. Scriven, V. C. Smith, R. M. Meloche, and A. M. J. Buchan The Role of Protein Kinase C Isozymes in Bombesin-stimulated Gastrin Release from Human Antral Gastrin Cells J. Biol. Chem., August 6, 1999; 274(32): 22493 - 22501. [Abstract] [Full Text] [PDF]
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R. T. Waldron, T. Iglesias, and E. Rozengurt The Pleckstrin Homology Domain of Protein Kinase D Interacts Preferentially with the eta Isoform of Protein Kinase C J. Biol. Chem., April 2, 1999; 274(14): 9224 - 9230. [Abstract] [Full Text] [PDF]
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L. Paolucci and E. Rozengurt Protein Kinase D in Small Cell Lung Cancer Cells: Rapid Activation through Protein Kinase C Cancer Res., February 1, 1999; 59(3): 572 - 577. [Abstract] [Full Text] [PDF]
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T. Iglesias, R. T. Waldron, and E. Rozengurt Identification of in Vivo Phosphorylation Sites Required for Protein Kinase D Activation J. Biol. Chem., October 16, 1998; 273(42): 27662 - 27667. [Abstract] [Full Text] [PDF]
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K. Nishikawa, A. Toker, K. Wong, P. A. Marignani, F.-J. Johannes, and L. C. Cantley Association of Protein Kinase Cµ with Type II Phosphatidylinositol 4-Kinase and Type I Phosphatidylinositol-4-phosphate 5-Kinase J. Biol. Chem., September 4, 1998; 273(36): 23126 - 23133. [Abstract] [Full Text] [PDF]
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E. Rozengurt V. Gastrointestinal peptide signaling through tyrosine phosphorylation of focal adhesion proteins Am J Physiol Gastrointest Liver Physiol, August 1, 1998; 275(2): G177 - G182. [Abstract] [Full Text] [PDF]
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D. Vertommen, M. Rider, Y. Ni, E. Waelkens, W. Merlevede, J. R. Vandenheede, and J. Van Lint Regulation of Protein Kinase D by Multisite Phosphorylation. IDENTIFICATION OF PHOSPHORYLATION SITES BY MASS SPECTROMETRY AND CHARACTERIZATION BY SITE-DIRECTED MUTAGENESIS J. Biol. Chem., June 23, 2000; 275(26): 19567 - 19576. [Abstract] [Full Text] [PDF]
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J. Sinnett-Smith, C. Santiskulvong, J. Duque, and E. Rozengurt [D-Arg1,D-Trp5,7,9,Leu11]Substance P Inhibits Bombesin-induced Mitogenic Signal Transduction Mediated by Both Gq and G12 in Swiss 3T3 Cells J. Biol. Chem., September 22, 2000; 275(39): 30644 - 30652. [Abstract] [Full Text] [PDF]
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T. Iglesias, N. Cabrera-Poch, M. P. Mitchell, T. J. P. Naven, E. Rozengurt, and G. Schiavo Identification and Cloning of Kidins220, a Novel Neuronal Substrate of Protein Kinase D J. Biol. Chem., December 15, 2000; 275(51): 40048 - 40056. [Abstract] [Full Text] [PDF]
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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., August 24, 2001; 276(35): 32606 - 32615. [Abstract] [Full Text] [PDF]
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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., August 24, 2001; 276(35): 32616 - 32626. [Abstract] [Full Text] [PDF]
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