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PMID: 9045612 Published · ppublish English Journal Article

PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism.

Science (New York, N.Y.) ·Vol. 275 ·No. 5305 ·1997-03-07 ·Pages 1475-8

Printen JA, Brady MJ, Saltiel AR

Abstract

Protein dephosphorylation by phosphatase PP1 plays a central role in mediating the effects of insulin on glucose and lipid metabolism. A PP1C-targeting protein expressed in 3T3-L1 adipocytes (called PTG, for protein targeting to glycogen) was cloned and characterized. PTG was expressed predominantly in insulin-sensitive tissues. In addition to binding and localizing PP1C to glycogen, PTG formed complexes with phosphorylase kinase, phosphorylase a, and glycogen synthase, the primary enzymes involved in the hormonal regulation of glycogen metabolism. Overexpression of PTG markedly increased basal and insulin-stimulated glycogen synthesis in Chinese hamster ovary cells overexpressing the insulin receptor, which do not express endogenous PTG. These results suggest that PTG is critical for glycogen metabolism, possibly functioning as a molecular scaffold.

MeSH Terms
3T3 Cells Amino Acid Sequence Animals CHO Cells Carrier Proteins/chemistry,genetics,metabolism Cloning, Molecular Cricetinae DNA, Complementary/genetics Glycogen/biosynthesis,metabolism Glycogen Synthase/metabolism Insulin/pharmacology Intracellular Signaling Peptides and Proteins Mice Molecular Sequence Data Phosphoprotein Phosphatases/metabolism Phosphorylase Kinase/metabolism Phosphorylase a/metabolism Phosphorylation Protein Binding Protein Phosphatase 1 Recombinant Fusion Proteins/metabolism Substrate Specificity Transfection
Chemicals
Carrier Proteins DNA, Complementary Insulin Intracellular Signaling Peptides and Proteins Ppp1r3c protein, mouse Recombinant Fusion Proteins Glycogen Phosphorylase a Glycogen Synthase Phosphorylase Kinase Phosphoprotein Phosphatases Protein Phosphatase 1
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Printen J A
Department of Physiology, University of Michigan School of Medicine, Ann Arbor, MI 48109, USA.
Brady M J
Saltiel A R
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1997-03-07
Pages
1475-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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