Journal article
Identification of the insulin-regulated interaction of phosphodiesterase 3B with 14-3-3 β protein
Diabetes (New York, N.Y.), Vol.51(12), pp.3362-3367
2002
DOI: 10.2337/diabetes.51.12.3362
PMID: 12453887
Abstract
Phosphodiesterase (PDE)-3B, a major PDE isoform in adipocytes, plays a pivotal role in the antilipolytic action of insulin. Insulin-induced phosphorylation and activation of PDE3B is phosphatidylinositol 3-kinase (PI3-K) and Akt dependent, but the precise mechanism of PDE3B activation is not fully understood. We have identified 14-3-3 β, a critical scaffolding molecule in signal transduction, as a protein that interacts with PDE3B using the yeast two-hybrid system. The interaction between PDE3B and 14-3-3 β was then confirmed in vitro. The glutathione S-transferase (GST)-tagged 14-3-3 β interacts with endogenous PDE3B of rat adipocytes, and this interaction is enhanced when adipocytes are treated with insulin. Coimmunoprecipitation experiments reveal that endogenous PDE3B also associates with endogenous 14-3-3 β in rat adipocytes, and this interaction is enhanced by insulin. Two different PI3-K inhibitors, wortmannin and Ly294002, block this induction, suggesting that PI3-K is required. Synthetic 15 amino acid peptides of rat PDE3B containing phosphorylated Ser-279 or -302 inhibit this interaction, indicating that the insulin-regulated phosphorylation of these serine residues is involved. Because insulin receptor substrate-1 also associates with 14-3-3, the dimeric 14-3-3 β could function as a scaffolding protein in the activation of PDE3B by insulin.
Details
- Title: Subtitle
- Identification of the insulin-regulated interaction of phosphodiesterase 3B with 14-3-3 β protein
- Creators
- Hiroshi ONUMA - Department of Laboratory Medicine, Ehime University School of Medicine, Ehime, JapanHaruhiko OSAWA - Department of Laboratory Medicine, Ehime University School of Medicine, Ehime, JapanKazuya YAMADA - Department of Biochemistry, Fukui Medical University and CREST, Japan Science and Technology, Fukui, JapanTakahiro OGURA - Department of Laboratory Medicine, Ehime University School of Medicine, Ehime, JapanFumiko TANABE - Department of Laboratory Medicine, Ehime University School of Medicine, Ehime, JapanDaryl K GRANNER - Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee, United StatesHideichi MAKINO - Department of Laboratory Medicine, Ehime University School of Medicine, Ehime, Japan
- Resource Type
- Journal article
- Publication Details
- Diabetes (New York, N.Y.), Vol.51(12), pp.3362-3367
- DOI
- 10.2337/diabetes.51.12.3362
- PMID
- 12453887
- NLM abbreviation
- Diabetes
- ISSN
- 0012-1797
- eISSN
- 1939-327X
- Publisher
- American Diabetes Association; Alexandria, VA
- Language
- English
- Date published
- 2002
- Academic Unit
- Molecular Physiology and Biophysics
- Record Identifier
- 9984020856502771
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