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Annu. Rev. Biophys. Biomol. Struct. 29 (1): 49-79
Copyright © 2000 by Annual Reviews.
Annu. Rev. Biophys. Biomol. Struct. 2000. 29:49-79.
SIGNALING AND SUBCELLULAR TARGETING BY MEMBRANE-BINDING DOMAINS
James H. Hurley and Saurav Misra
Laboratory of Molecular Biology, National Institute of Diabetes and
Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0580; e-mail: jh8e{at}nih.gov
C1 domain, C2 domain, FYVE domain, PH domain, subcellular localization
Protein kinase C homology-1 and -2, FYVE, and pleckstrin homology
domains are ubiquitous in eukaryotic signal transduction and
membrane-trafficking proteins. These domains regulate
subcellular localization and protein function by binding to lipid
ligands embedded in cell membranes. Structural and biochemical
analysis of these domains has shown that their molecular mechanisms
of membrane binding depend on a combination of specific and
nonspecific interactions with membrane lipids. In vivo studies
of green fluorescent protein fusions have highlighted the key roles
of these domains in regulating protein localization to plasma and
internal membranes in cells.
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