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Phosphorylation of phosphoprotein phosphatase inhibitor-2 (I-2) in rat fat cells.

作者信息

Lawrence J C, Hiken J, Burnette B, DePaoli-Roach A A

机构信息

Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.

出版信息

Biochem Biophys Res Commun. 1988 Jan 15;150(1):197-203. doi: 10.1016/0006-291x(88)90505-0.

DOI:10.1016/0006-291x(88)90505-0
PMID:2827665
Abstract

Fat cells were incubated with 32Pi for 2 h before the [32P]I-2 was immunoprecipitated, subjected to SDS/PAGE, and detected by autoradiography. [32P]I-2 (Mr = 32,000) was not recovered when excess purified I-2 was added with the antiserum or when nonimmune serum was used. Immunoprecipitated I-2 was heat-stable, inhibited phosphatase activity, and could be synergistically phosphorylated by casein kinase II and FA/GSK-3. Several times more [32P]phosphoserine than [32P]phosphothreonine was found in I-2 from 32P-labeled cells. Insulin increased the 32P-content of I-2 by as much as 40%, suggesting that phosphorylation of I-2 might be involved in the effect of insulin on stimulating protein dephosphorylation.

摘要

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