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PMID: 6125415 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Role of insulin-stimulated protein phosphorylation in insulin action.

Federation proceedings ·Vol. 41 ·No. 10 ·1982-08-00 ·Pages 2629-33

Avruch J, Alexander MC, Palmer JL, Pierce MW, Nemenoff RA, Blackshear PJ, Tipper JP, Witters LA

Abstract

Insulin promotes both the phosphorylation and dephosphorylation of proteins in its target cells. Insulin-induced dephosphorylation has long been thought to serve an important regulatory function; the role of insulin-stimulation phosphorylation is less certain. The proteins known to be substrates for this reaction are ATP citrate (pro-3S)-lyase, acetyl-CoA carboxylase, and the ribosomal subunit S6. The evidence as to the physiological role and mechanism underlying the insulin-stimulated phosphorylation of these proteins is summarized. Present information suggests that insulin-stimulated phosphorylation may serve an important regulatory role in certain actions of insulin.

MeSH Terms
ATP Citrate (pro-S)-Lyase/metabolism Acetyl-CoA Carboxylase/metabolism Animals Calcium/physiology Calmodulin/physiology Cyclic AMP/physiology Insulin/physiology Ligases/metabolism Liver/metabolism Muscles/metabolism Phosphorylation Protein Kinases/metabolism Rats Ribosomal Protein S6 Ribosomal Proteins/metabolism
Chemicals
Calmodulin Insulin Ribosomal Protein S6 Ribosomal Proteins Cyclic AMP ATP Citrate (pro-S)-Lyase Protein Kinases Ligases Acetyl-CoA Carboxylase Calcium
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Avruch J
Alexander M C
Palmer J L
Pierce M W
Nemenoff R A
Blackshear P J
Tipper J P
Witters L A
Article Info
Journal
Federation proceedings
Abbr.
Fed Proc
ISSN
0014-9446
Published
1982-08-00
Pages
2629-33
Language
English
Region
United States
NLM ID
0372771
Subset
IM
Grants
NIADDK NIH HHS · AM17776 · United States
NIADDK NIH HHS · AM19270 · United States
NIADDK NIH HHS · AM26041 · United States
External Links
PubMed source
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