
Eva Degerman
Professor

Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor
Author
Summary, in 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.
Department/s
- Insulin Signal Transduction
Publishing year
2000
Language
English
Pages
10093-10098
Publication/Series
Journal of Biological Chemistry
Volume
275
Issue
14
Links
Document type
Journal article
Publisher
ASBMB
Topic
- Endocrinology and Diabetes
Status
Published
Research group
- Insulin Signal Transduction
ISBN/ISSN/Other
- ISSN: 1083-351X