Identification of a novel class of mammalian phosphoinositol-specific phospholipase C enzymes.

Alan James Stewart, J Mukherjee, SJ Roberts, D Lester, C Farquharson

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)

Abstract

Phosphoinositol (PhoIns)-specific phospholipase C enzymes (PLCs) are central to the inositol lipid signaling pathways and contribute to intracellular Ca2+ release and protein kinase C activation. Five distinct classes of PhoIns-specific PLCs are known to exist in mammals, which are activated by membrane receptor-mediated events. Here we have identified a sixth class of PhoIns-specific PLC with a novel domain structure, which we have termed PLC-eta. Two putative PLC-eta enzymes were identified in humans and in mice. Sequence analysis revealed that residues implicated in substrate binding and catalysis from other PhoIns-specific PLCs are conserved in the novel enzymes. PLC-eta enzymes are most closely related to the PLC-delta class and share a close evolutionary relationship with other PLC isozymes. EST analysis and RT-PCR data suggest that PLC-eta enzymes are expressed in several cell types and, by analogy with other mammalian PhoIns-specific PLCs, are likely to be involved in signal transduction pathways.
Original languageEnglish
Pages (from-to)117-121
JournalInternational Journal of Molecular Medicine
Volume15
DOIs
Publication statusPublished - Jan 2005

Keywords

  • Ca2+ Signaling
  • Phosphatidylinositol
  • Phospholipase C-eta
  • Protein Kinase C
  • Receptor-Mediated Signaling
  • Signal Transduction
  • Ca2+ signaling
  • phosphatidylinositol
  • phospholipase C-eta
  • protein kinase C
  • receptor-mediated signaling
  • signal transduction
  • PLECKSTRIN HOMOLOGY DOMAINS
  • BETA-GAMMA-SUBUNITS
  • PROTEIN-KINASE-C
  • TRANSCRIPTIONAL ACTIVATION
  • CA2+ OSCILLATIONS
  • CATALYTIC DOMAIN
  • BIND
  • PLC

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