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PLC regulation: emerging pictures for molecular mechanisms

Bunney, TD; Katan, M; (2011) PLC regulation: emerging pictures for molecular mechanisms. TRENDS BIOCHEM SCI , 36 (2) 88 - 96. 10.1016/j.tibs.2010.08.003.

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Abstract

Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.

Type: Article
Title: PLC regulation: emerging pictures for molecular mechanisms
DOI: 10.1016/j.tibs.2010.08.003
Keywords: PHOSPHOLIPASE-C-GAMMA, PLECKSTRIN HOMOLOGY DOMAIN, TYROSINE KINASE, LIVING CELLS, CRYSTAL-STRUCTURE, RHO GTPASES, MEMBRANE, RECEPTOR, ACTIVATION, ISOZYMES
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1326660
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