Families of phosphoinositide-specific phospholipase C: structure and function

Authors
Citation
M. Katan, Families of phosphoinositide-specific phospholipase C: structure and function, BBA-MOL C B, 1436(1-2), 1998, pp. 5-17
Citations number
98
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
ISSN journal
13881981 → ACNP
Volume
1436
Issue
1-2
Year of publication
1998
Pages
5 - 17
Database
ISI
SICI code
1388-1981(199812)1436:1-2<5:FOPPCS>2.0.ZU;2-F
Abstract
A large number of extracellular signals stimulate hydrolysis of phosphatidy linositol 4,5-bisphosphate by phosphoinositide-specific phospholipase C (PI -PLC). PI-PLC isozymes have been found in a broad spectrum of organisms and although they have common catalytic properties, their regulation involves different signalling pathways, A number of recent studies provided an insig ht into domain organisation of PI-PLC isozymes and contributed towards bett er understanding of the structural basis for catalysis, cellular localisati on and molecular changes that could underlie the process of their activatio n. (C) 1998 Elsevier Science B.V. All rights reserved.