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

Research output: Contribution to journalArticlepeer-review

DOI

Author(s)

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

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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.
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Original languageEnglish
Pages (from-to)117-121
JournalInternational Journal of Molecular Medicine
Volume15
DOIs
Publication statusPublished - Jan 2005

    Research areas

  • 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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