Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction

Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction A serine/threonine kinase, named protein kinase B (PKB)1 for its sequence homology to both protein kinase A and C, has previously been isolated. PKB, which is identical to the kinase Rac2, was later found to be the cellular homologue of the transforming v-Akt3. Here we show that PKB is activated by stimuli such as insulin, platelet-derived growth factor (PDGF), epidermal growth factor (EGF) and basic fibroblast growth factor (bFGF). Activation of PKB was inhibited by the phosphatidylinositol-3-OH kinase (PI(3)K) inhibitor wortmannin and by coexpression of a dominant-negative mutant of PI(3)K. PDGF receptor mutants that lack detectable associated PI(3)K activity also fail to induce PKB activation. PKB kinase activity is correlated with phosphorylation of PKB on serine. Finally, we show that a constructed Gag–PKB fusion protein, homologous to the v-akt oncogene, displays significantly increased ligand-independent kinase activity. Furthermore, this activity is sufficient to activate the p70 S6-kinase (p70S6k). These results suggest a role for PKB in PI(3)K-mediated signal transduction. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction

Burgering, Boudewijn M. Th.; Coffer, Paul J.
Nature , Volume 376 (6541) – Aug 17, 1995
Download PDF
4 pages

Loading next page...
 
/lp/springer-journals/protein-kinase-b-c-akt-in-phosphatidylinositol-3-oh-kinase-signal-px9147Lb2c

References (18)

Publisher
Springer Journals
Copyright
Copyright © 1995 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/376599a0
Publisher site
See Article on Publisher Site

Abstract

A serine/threonine kinase, named protein kinase B (PKB)1 for its sequence homology to both protein kinase A and C, has previously been isolated. PKB, which is identical to the kinase Rac2, was later found to be the cellular homologue of the transforming v-Akt3. Here we show that PKB is activated by stimuli such as insulin, platelet-derived growth factor (PDGF), epidermal growth factor (EGF) and basic fibroblast growth factor (bFGF). Activation of PKB was inhibited by the phosphatidylinositol-3-OH kinase (PI(3)K) inhibitor wortmannin and by coexpression of a dominant-negative mutant of PI(3)K. PDGF receptor mutants that lack detectable associated PI(3)K activity also fail to induce PKB activation. PKB kinase activity is correlated with phosphorylation of PKB on serine. Finally, we show that a constructed Gag–PKB fusion protein, homologous to the v-akt oncogene, displays significantly increased ligand-independent kinase activity. Furthermore, this activity is sufficient to activate the p70 S6-kinase (p70S6k). These results suggest a role for PKB in PI(3)K-mediated signal transduction.

Journal

Nature – Springer Journals

Published: Aug 17, 1995

There are no references for this article.