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Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor

Author:
  • C M Rondinone
  • E Carvalho
  • T Rahn
  • V C Manganiello
  • Eva Degerman
  • U P Smith
Publishing year: 2000
Language: English
Pages: 10093-10098
Publication/Series: Journal of Biological Chemistry
Volume: 275
Issue: 14
Document type: Journal article
Publisher: ASBMB

Abstract english

Phosphatidylinositol 3-kinase mediates several actions of insulin including its antilipolytic effect. This effect is elicited by the insulin-stimulated serine phosphorylation and activation of cGMP-inhibited phosphodiesterase (PDE3B). In human adipocytes, we found that insulin differentially stimulated phosphatidylinositol 3-kinase activity; the lipid kinase activity was associated with IRS-1, whereas the serine kinase activity was associated with the insulin receptor and phosphorylated a number of proteins including p85, p110, and a 135-kDa protein identified as PDE3B. PDE3B phosphorylation was associated with enzyme activation, thus initiating the antilipolytic effect of insulin. These results show a novel pathway for intracellular signaling through the insulin receptor leading to the serine phosphorylation of key proteins involved in insulin action.

Keywords

  • Endocrinology and Diabetes

Other

Published
  • Insulin Signal Transduction
  • ISSN: 1083-351X
Eva Degerman
E-mail: eva.degerman [at] med.lu.se

Professor

Insulin Signal Transduction

+46 46 222 85 83

+46 70 885 83 62

BMC C1121b

66

Lund University Diabetes Centre, CRC, SUS Malmö, Entrance 72, House 91:12. SE-205 02 Malmö. Telephone: +46 40 39 10 00