Format

Send to

Choose Destination
Biochim Biophys Acta. 1998 Dec 8;1436(1-2):5-17.

Families of phosphoinositide-specific phospholipase C: structure and function.

Author information

1
CRC Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK. matilda@icr.ac.uk

Abstract

A large number of extracellular signals stimulate hydrolysis of phosphatidylinositol 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 insight into domain organisation of PI-PLC isozymes and contributed towards better understanding of the structural basis for catalysis, cellular localisation and molecular changes that could underlie the process of their activation.

PMID:
9838022
DOI:
10.1016/s0005-2760(98)00125-8
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center