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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 orcid 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)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
275
issue
14
pages
10093 - 10098
publisher
American Society for Biochemistry and Molecular Biology
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
2016-04-01 12:10:15
date last changed
2022-01-26 23:47:31
@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    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor}},
  url          = {{http://www.jbc.org/cgi/content/abstract/275/14/10093}},
  volume       = {{275}},
  year         = {{2000}},
}