Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1-Reference-Cited by-同舟云学术

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

Published:1998-09-25 Issue:5385 Volume:281 Page:2042-2045
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Le Good J. Ann¹,Ziegler Wolfgang H.¹,Parekh Davey B.¹,Alessi Dario R.¹,Cohen Philip¹,Parker Peter J.¹

Affiliation:

1. 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.

Abstract

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 PKCζ and PKCδ 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 PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase–dependent and was enhanced by PDK1 coexpression.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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