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PMID: 9838022 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

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

Biochimica et biophysica acta ·Vol. 1436 ·No. 1-2 ·1998-12-08 ·Pages 5-17

Katan M

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.

MeSH Terms
Animals Hydrolysis Isoenzymes/chemistry,metabolism Models, Molecular Phosphatidylinositol Diacylglycerol-Lyase Phosphatidylinositols/metabolism Phosphoinositide Phospholipase C Phospholipase C beta Phospholipase C gamma Phosphoric Diester Hydrolases/chemistry,metabolism Type C Phospholipases/chemistry,metabolism
Chemicals
Isoenzymes Phosphatidylinositols Phosphoric Diester Hydrolases Type C Phospholipases Phosphoinositide Phospholipase C Phospholipase C beta Phospholipase C gamma Phosphatidylinositol Diacylglycerol-Lyase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Katan M
CRC Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK. [email protected]
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1998-12-08
Pages
5-17
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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