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Biochem J. 2005 Nov 1;391(Pt 3):e7-9.

New insights into the families of PLC enzymes: looking back and going forward.

Author information

  • 1Cancer Research UK Centre for Cell and Molecular Biology, Chester Beatty Laboratories, The Institute of Cancer Research, Fulham Road, London, SW3 6JB, UK. matilda@icr.ac.uk

Abstract

A study in this issue of the Biochemical Journal by Harden and colleagues, in association with one published in the Biochemical Journal very recently [Hwang, Oh, Shin, Kim, Ryu and Suh (2005) Biochem. J. 389, 181-186], have defined a new member of the superfamily of PLC (phosphoinositide-specific phospholipase C) enzymes, PLCeta. Two isoforms, PLCeta1 and PLCeta2, and their splice variants add to the molecular diversity of PLC enzymes. The studies of PLCeta regulation suggest that at least some splice variants of PLCeta2 could be regulated by the G-protein subunits Gbetagamma. As two other families, PLCbeta and PLC, are also regulated through heterotrimeric G-proteins, this finding reveals further complexity and possible interplay between different PLC families and their regulatory networks. At this point, when it is likely that the PLCeta family completes the effort of identifying new members of this related group of PLC enzymes, I also discuss some more general concepts of PLC regulation and catalysis, and challenges awaiting their further studies.

PMID:
16238548
PMCID:
PMC1276975
DOI:
10.1042/BJ20051506
[PubMed - indexed for MEDLINE]
Free PMC Article
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