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Physiological Reviews, Vol. 80, No. 4, October 2000, pp. 1291-1335
Copyright ©2000 by the American Physiological Society
Departments of Anesthesiology and Physiology and Biophysics, School of Medicine, State University of New York, Stony Brook, New York
Rebecchi, Mario J. and
Srinivas N. Pentyala.
Structure, Function, and Control of
Phosphoinositide-Specific Phospholipase C. Physiol. Rev. 80: 1291-1335, 2000.
Phosphoinositide-specific
phospholipase C (PLC) subtypes
,
, and
comprise a related
group of multidomain phosphodiesterases that cleave the polar head
groups from inositol lipids. Activated by all classes of cell surface
receptor, these enzymes generate the ubiquitous second messengers
inositol 1,4,5-trisphosphate and diacylglycerol. The last 5 years have
seen remarkable advances in our understanding of the molecular and
biological facets of PLCs. New insights into their multidomain
arrangement and catalytic mechanism have been gained from
crystallographic studies of PLC-
1 , while new modes of
controlling PLC activity have been uncovered in cellular studies. Most
notable is the realization that PLC-
, -
, and -
isoforms act in
concert, each contributing to a specific aspect of the cellular
response. Clues to their true biological roles were also obtained. Long
assumed to function broadly in calcium-regulated processes, genetic
studies in yeast, slime molds, plants, flies, and mammals point to
specific and conditional roles for each PLC isoform in cell signaling
and development. In this review we consider each subtype of PLC in
organisms ranging from yeast to mammals and discuss their molecular
regulation and biological function.
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