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Science 25 September 1998:
Vol. 281. no. 5385, pp. 2042 - 2045
DOI: 10.1126/science.281.5385.2042
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Reports

Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1

J. Ann Le Good, * Wolfgang H. Ziegler, * Davey B. Parekh, Dario R. Alessi, Philip Cohen, Peter J. Parker dagger

Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCzeta and PKCdelta in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1. PDK1-dependent phosphorylation of PKCdelta in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCdelta in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.

J. A. Le Good, W. H. Ziegler, D. B. Parekh, P. J. Parker, Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK. D. R. Alessi, and P. Cohen, Department of Biochemistry, Medical Sciences Institute, Dundee University, Dundee DD1 4HN, UK.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed.

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Oxidative Activation of Protein Kinase C{gamma} through the C1 Domain: EFFECTS ON GAP JUNCTIONS.
D. Lin and D. J. Takemoto (2005)
J. Biol. Chem. 280, 13682-13693
   Abstract »    Full Text »    PDF »
PDK1 Nucleates T Cell Receptor-Induced Signaling Complex for NF-{kappa}B Activation.
K.-Y. Lee, F. D'Acquisto, M. S. Hayden, J.-H. Shim, and S. Ghosh (2005)
Science 308, 114-118
   Abstract »    Full Text »    PDF »
Relaxin Stimulates Protein Kinase C {zeta} Translocation: Requirement for Cyclic Adenosine 3',5'-Monophosphate Production.
B. T. Nguyen and C. W. Dessauer (2005)
Mol. Endocrinol. 19, 1012-1023
   Abstract »    Full Text »    PDF »
Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling.
W. von Stein, A. Ramrath, A. Grimm, M. Muller-Borg, and A. Wodarz (2005)
Development 132, 1675-1686
   Abstract »    Full Text »    PDF »
Phosphoinositide-Dependent Phosphorylation of PDK1 Regulates Nuclear Translocation.
M. P. Scheid, M. Parsons, and J. R. Woodgett (2005)
Mol. Cell. Biol. 25, 2347-2363
   Abstract »    Full Text »    PDF »
Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC.
T. Seki, H. Matsubayashi, T. Amano, Y. Shirai, N. Saito, and N. Sakai (2005)
Genes Cells 10, 225-239
   Abstract »    Full Text »    PDF »
Insulin potentiates AVP-induced AQP2 expression in cultured renal collecting duct principal cells.
M. Bustamante, U. Hasler, O. Kotova, A. V. Chibalin, D. Mordasini, M. Rousselot, A. Vandewalle, P.-Y. Martin, and E. Feraille (2005)
Am J Physiol Renal Physiol 288, F334-F344
   Abstract »    Full Text »    PDF »
Insulin-like growth factor-I receptor signalling and acquired resistance to gefitinib (ZD1839; Iressa) in human breast and prostate cancer cells.
H E Jones, L Goddard, J M W Gee, S Hiscox, M Rubini, D Barrow, J M Knowlden, S Williams, A E Wakeling, and R I Nicholson (2004)
Endocr. Relat. Cancer 11, 793-814
   Abstract »    Full Text »    PDF »
Primary granule release from human neutrophils is potentiated by soluble fibrinogen through a mechanism depending on multiple intracellular signaling pathways.
F. Tuluc, A. Garcia, O. Bredetean, J. Meshki, and S. P. Kunapuli (2004)
Am J Physiol Cell Physiol 287, C1264-C1272
   Abstract »    Full Text »    PDF »
Protein Phosphatase 2A Negatively Regulates Insulin's Metabolic Signaling Pathway by Inhibiting Akt (Protein Kinase B) Activity in 3T3-L1 Adipocytes.
S. Ugi, T. Imamura, H. Maegawa, K. Egawa, T. Yoshizaki, K. Shi, T. Obata, Y. Ebina, A. Kashiwagi, and J. M. Olefsky (2004)
Mol. Cell. Biol. 24, 8778-8789
   Abstract »    Full Text »    PDF »
Differential roles of PDK1- and PDK2-phosphorylation sites in the yeast AGC kinases Ypk1, Pkc1 and Sch9.
F. M. Roelants, P. D. Torrance, and J. Thorner (2004)
Microbiology 150, 3289-3304
   Abstract »    Full Text »    PDF »
Tissue-Specific Differences in Activation of Atypical Protein Kinase C and Protein Kinase B in Muscle, Liver, and Adipocytes of Insulin Receptor Substrate-1 Knockout Mice.
M. P. Sajan, M. L. Standaert, A. Miura, C. R. Kahn, and R. V. Farese (2004)
Mol. Endocrinol. 18, 2513-2521
   Abstract »    Full Text »    PDF »
The SH3-SAM Adaptor HACS1 is Up-regulated in B Cell Activation Signaling Cascades.
Y. X. Zhu, S. Benn, Z. H. Li, E. Wei, E. Masih-Khan, Y. Trieu, M. Bali, C. J. McGlade, J. O. Claudio, and A. K. Stewart (2004)
J. Exp. Med. 200, 737-747
   Abstract »    Full Text »    PDF »
Role of protein kinase C{zeta} in thrombin-induced endothelial permeability changes: inhibition by angiopoietin-1.
X. Li, C. N. Hahn, M. Parsons, J. Drew, M. A. Vadas, and J. R. Gamble (2004)
Blood 104, 1716-1724
   Abstract »    Full Text »    PDF »
Activation of PI3K Is Indispensable for Interleukin 7-mediated Viability, Proliferation, Glucose Use, and Growth of T Cell Acute Lymphoblastic Leukemia Cells.
J. T. Barata, A. Silva, J. G. Brandao, L. M. Nadler, A. A. Cardoso, and V. A. Boussiotis (2004)
J. Exp. Med. 200, 659-669
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Encapsulated Streptococcus suis Inhibits Activation of Signaling Pathways Involved in Phagocytosis.
M. Segura, M. Gottschalk, and M. Olivier (2004)
Infect. Immun. 72, 5322-5330
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Role of Atypical Protein Kinase C in Estradiol-Triggered G1/S Progression of MCF-7 Cells.
G. Castoria, A. Migliaccio, M. Di Domenico, M. Lombardi, A. de Falco, L. Varricchio, A. Bilancio, M. V. Barone, and F. Auricchio (2004)
Mol. Cell. Biol. 24, 7643-7653
   Abstract »    Full Text »    PDF »
Regulation and Function of Cyclin D2 in B Lymphocyte Subsets.
T. C. Chiles (2004)
J. Immunol. 173, 2901-2907
   Abstract »    Full Text »    PDF »


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