The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Structure, Function, and Control of Phosphoinositide-Specific Phospholipase C
Abstract
Phosphoinositide-specific phospholipase C (PLC) subtypes β, γ, and δ 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-δ 1, while new modes of controlling PLC activity have been uncovered in cellular studies. Most notable is the realization that PLC-β, -γ, and -δ 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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Citations
Cites
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Phospholipase C isozymes selectively couple to specific neurotransmitter receptors
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Cited by
AKAP signalling complexes: focal points in space and time
Wong, W., & Scott, J. D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1527 · Cited by 1,073
Plasma membrane phosphoinositide organization by protein electrostatics
McLaughlin, S., & Murray, D. (2005) · Nature · doi:10.1038/nature04398 · Cited by 868
PIP2and Proteins: Interactions, Organization, and Information Flow
McLaughlin, S., Wang, J., Gambhir, A., & Murray, D. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134259 · Cited by 837
Phospholipid-Based Signaling in Plants
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Metadata
- Authors
- Rebecchi, M. J., & Pentyala, S. N.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2000-01-10
- Volume
- 80
- Issue
- 4
- Pages
- 1291-1335
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2096549360
- Cited by
- 997
- References
- 9
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- closed
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