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

Rondinone, C M; Carvalho, E; Rahn, T; Manganiello, V C; Degerman, Eva LU and Smith, U P (2000) In Journal of Biological Chemistry 275(14). p.10093-10098
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
275
issue
14
pages
10093 - 10098
publisher
ASBMB
external identifiers
  • pmid:10744689
  • scopus:0034616384
ISSN
1083-351X
language
English
LU publication?
yes
id
cd70e804-7680-47b7-89ba-3836240c459f (old id 1117976)
alternative location
http://www.jbc.org/cgi/content/abstract/275/14/10093
date added to LUP
2008-06-25 08:25:33
date last changed
2017-01-01 04:54:21
@article{cd70e804-7680-47b7-89ba-3836240c459f,
  abstract     = {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.},
  author       = {Rondinone, C M and Carvalho, E and Rahn, T and Manganiello, V C and Degerman, Eva and Smith, U P},
  issn         = {1083-351X},
  language     = {eng},
  number       = {14},
  pages        = {10093--10098},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor},
  volume       = {275},
  year         = {2000},
}