Phosphorylation of PDE3B by phosphatidylinositol 3-kinase associated with the insulin receptor
(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:
https://lup.lub.lu.se/record/1117976
- author
- Rondinone, C M
; Carvalho, E
; Rahn, T
; Manganiello, V C
; Degerman, Eva
LU
and Smith, U P
- organization
- publishing date
- 2000
- 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}}, }