Identification of a novel class of mammalian phosphoinositol-specific phospholipase C enzymes |
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Authors: | Stewart Alan J Mukherjee Joy Roberts Scott J Lester Douglas Farquharson Colin |
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Affiliation: | Division of Gene Function and Development, Roslin Institute, Roslin, Midlothian EH25 9PS, UK. alan.stewart@bbsrc.ac.uk |
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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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