Mammalian phospholipase C

Ganesh Kadamur, Elliott M. Ross

Research output: Contribution to journalReview article

192 Scopus citations

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

Keywords

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

ASJC Scopus subject areas

  • Physiology

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