Mammalian phospholipase C

Ganesh Kadamur, Elliott M. Ross

Research output: Contribution to journalArticle

166 Citations (Scopus)

Abstract

Phospholipase C (PLC) converts phosphatidylinositol 4,5-bisphosphate (PIP2) to inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). DAG and IP3 each control diverse cellular processes and are also substrates for synthesis of other important signaling molecules. PLC is thus central to many important interlocking regulatory networks. Mammals express six families of PLCs, each with both unique and overlapping controls over expression and subcellular distribution. Each PLC also responds acutely to its own spectrum of activators that includes heterotrimeric G protein subunits, protein tyrosine kinases, small G proteins, Ca2+, and phospholipids. Mammalian PLCs are autoinhibited by a region in the catalytic TIM barrel domain that is the target of much of their acute regulation. In combination, the PLCs act as a signaling nexus that integrates numerous signaling inputs, critically governs PIP2 levels, and regulates production of important second messengers to determine cell behavior over the millisecond to hour timescale.

Original languageEnglish (US)
Pages (from-to)127-154
Number of pages28
JournalAnnual Review of Physiology
Volume75
DOIs
StatePublished - Feb 10 2013

Fingerprint

Type C Phospholipases
Diglycerides
Heterotrimeric GTP-Binding Proteins
Inositol 1,4,5-Trisphosphate
Monomeric GTP-Binding Proteins
Protein Subunits
Second Messenger Systems
Phosphatidylinositols
Protein-Tyrosine Kinases
Mammals
Catalytic Domain
Phospholipids

Keywords

  • Ca
  • Diacylglycerol
  • G protein
  • Inositol 1,4,5-trisphosphate
  • Phosphatidylinositol 4,5-bisphosphate
  • Protein tyrosine kinase

ASJC Scopus subject areas

  • Physiology

Cite this

Mammalian phospholipase C. / Kadamur, Ganesh; Ross, Elliott M.

In: Annual Review of Physiology, Vol. 75, 10.02.2013, p. 127-154.

Research output: Contribution to journalArticle

Kadamur, Ganesh ; Ross, Elliott M. / Mammalian phospholipase C. In: Annual Review of Physiology. 2013 ; Vol. 75. pp. 127-154.
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