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

  • 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.


  • Endocrinology and Diabetes


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


Insulin Signal Transduction

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