Publication Date:
1998-09-25
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le Good, J A -- Ziegler, W H -- Parekh, D B -- Alessi, D R -- Cohen, P -- Parker, P J -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748166" target="_blank"〉PubMed〈/a〉
Keywords:
3-Phosphoinositide-Dependent Protein Kinases
;
Binding Sites
;
Cell Line
;
Chromones/pharmacology
;
Enzyme Activation
;
Enzyme Inhibitors/pharmacology
;
Humans
;
Isoenzymes/*metabolism
;
Morpholines/pharmacology
;
Phosphatidylcholines/pharmacology
;
Phosphatidylinositol 3-Kinases/*metabolism
;
Phosphatidylinositol Phosphates
;
Phosphatidylserines/pharmacology
;
Phosphorylation
;
Protein Kinase C/*metabolism
;
Protein Kinase C beta
;
Protein-Serine-Threonine Kinases/*metabolism
;
Recombinant Proteins/metabolism
;
Tetradecanoylphorbol Acetate/pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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