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Biochem Biophys Res Commun. 2001 Apr 6;282(3):839-43.

The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin.

Author information

1
Interdisciplinary Research Institute (IRIBHN), Université Libre de Bruxelles, Campus Erasme, 808 Route de Lennik, Brussels, 1070, Belgium.

Erratum in

  • Biochem Biophys Res Commun 2001 Jun 22;284(4):1090.

Abstract

The lipid phosphatase SHIP2 (SH2 domain containing inositol 5-phosphatase 2) has recently been shown to be a potent negative regulator of insulin signaling and insulin sensitivity in vivo. We show here that SHIP2 is expressed in Chinese hamster ovary cells overexpressing the insulin receptor (CHO-IR cells) and tyrosine phosphorylated upon insulin stimulation. We show that SHIP2, which is recruited in anti-phosphotyrosine immunoprecipitates in insulin-stimulated cells, accounts for the insulin sensitivity or apparent increase in activity reported by Guilherme et al. (J. Biol. Chem. 271, 29533-29536, 1996). Overexpression of SHIP2 led to a decrease of the insulin-dependent PIP3 production as well as Akt/PKB activation and MAPK stimulation.

PMID:
11401540
DOI:
10.1006/bbrc.2001.4639
[Indexed for MEDLINE]

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