2001年5月
Interaction of p130 with, and consequent inhibition of, the catalytic subunit of protein phosphatase 1 alpha
JOURNAL OF BIOLOGICAL CHEMISTRY
- 巻
- 276
- 号
- 21
- 開始ページ
- 17908
- 終了ページ
- 17913
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M009677200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The protein p130 was originally isolated from rat brain as an inositol 1,4,5-trisphosphate-binding protein with a domain organization similar to that of phospholipase C-delta1 but which lacks phospholipase C activity. Yeast two-hybrid screening of a human brain cDNA library for clones that encode proteins that interact with p130 has now led to the identification of the catalytic subunit of protein phosphatase 1 alpha (PP1c alpha) as a p130-binding protein. The association between p130 and PP1c alpha was also confirmed in vitro by an overlay assay, a "pull-down" assay, and surface plasmon resonance analysis. The interaction of p130 with PP1c alpha resulted in inhibition of the catalytic activity of the latter in a p130 concentration-dependent manner. Immunoprecipitation and immunoblot analysis of COS-1 cells that stably express p130 and of mouse brain extract with antibodies to p130 and to PP1c alpha also detected the presence of a complex of p130 and PP1c alpha, The activity of glycogen phosphorylase, which is negatively regulated by dephosphorylation by PP1c alpha, was higher in COS-1 cells that stably express p130 than in control COS-1 cells. These results suggest that, in addition to its role in inositol 1,4,5-trisphosphate and Ca2+ signaling, p130 might also contribute to regulation of protein dephosphorylation through its interaction with PP1c alpha.
- リンク情報
- ID情報
-
- DOI : 10.1074/jbc.M009677200
- ISSN : 0021-9258
- PubMed ID : 11278544
- Web of Science ID : WOS:000168866500041