Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-12

AUTHORS

M Camps, A Carozzi, P Schnabel, A Scheer, P J Parker, P Gierschik

ABSTRACT

Hydrolysis by phospholipase C (PLC) of phosphatidylinositol 4,5-bisphosphate is a key mechanism by which many extracellular signalling molecules regulate functions of their target cells. At least eight distinct isozymes of PLC are recognized in mammalian cells. Receptor-controlled PLC is often regulated by G proteins, which can be modified by pertussis toxin in some cells but not in others. In the latter cells, PLC-beta 1, but not PLC-gamma 1 or PLC-delta 1, may be activated by members of the alpha q-subfamily of the G protein alpha-subunits. An unidentified PLC in soluble fractions of cultured human HL-60 granulocytes is specifically stimulated by G protein beta gamma subunits purified from retina and brain. Identification of a second PLC-beta complementary DNA (PLC-beta 2) in an HL-60 cell cDNA library prompted us to investigate the effect of purified G protein beta gamma subunits on the activities of PLC-beta 1 and PLC-beta 2 transiently expressed in cultured mammalian cells. We report here that PLC-beta 1 and PLC-beta 2 were stimulated by free beta gamma subunits and that PLC-beta 2 was the most sensitive to beta gamma stimulation. Thus stimulation of PLC by beta gamma subunits is isozyme-selective and PLC-beta 2 is a prime target of beta gamma stimulation. Activation of PLC-beta 2 by beta gamma subunits may be an important mechanism by which pertussis toxin-sensitive G proteins stimulate PLC. More... »

PAGES

684-686

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/360684a0

DOI

http://dx.doi.org/10.1038/360684a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001203040

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1465133


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