Home LiteratureArticle Details
PMID: 8380773 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Activation of phosphatidylinositol lipid-specific phospholipase C-beta 3 by G-protein beta gamma subunits.

FEBS letters ·Vol. 315 ·No. 3 ·1993-01-11 ·Pages 340-2

Carozzi A, Camps M, Gierschik P, Parker PJ

Abstract

A novel member of the inositol lipid-specific phospholipase C family, PtdIns-PLC beta 3, is shown to be activated by beta gamma subunits of the heterotrimeric GTP-binding protein, transducin. The activation is a direct effect since it is observed with the purified proteins. Furthermore, the activation is blocked by the GDP-liganded alpha subunit of transducin, confirming that the effect is due to free beta gamma subunits. The implications with respect to receptor-PtdIns-PLC coupling are discussed.

MeSH Terms
Animals Blotting, Western Cattle Cell Line, Transformed Chlorocebus aethiops Enzyme Activation Isoenzymes/metabolism Phosphatidylinositol Diacylglycerol-Lyase Phosphoric Diester Hydrolases/metabolism Transducin/metabolism
Chemicals
Isoenzymes Phosphoric Diester Hydrolases Transducin Phosphatidylinositol Diacylglycerol-Lyase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Carozzi A
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London, UK.
Camps M
Gierschik P
Parker P J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1993-01-11
Pages
340-2
Language
English
Region
England
NLM ID
0155157
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com