Functions of the nuclear lamins |
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Authors: | O. A. Vaughan W. G. E. Whitfield C. J. Hutchison |
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Affiliation: | (1) Basel Institute for Immunology, Grenzacherstrasse 287, CH-4005 Basel, Switzerland;(2) Department of Molecular and Cell Biology, University of California at Berkeley, California |
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Abstract: | Summary Raft membrane domains are envisioned as lateral assemblies of cholesterol and sphingolipids which adopt a liquid-ordered membrane phase. Our understanding of the raft architecture in cell membranes is developing rapidly. The current view describes raft domains as small and highly dynamic subdomains of cell membranes. The size and stability of raft domains are essential parameters which determine the function of raft domains in cells. Here we discuss how the architecture and stability of raft domains is regulated by oligomerisation of raft components and by modulation of their molecular composition.Abbreviations DIGs detergent-insoluble glycolipid-enriched membranes - GPI glycosylphosphatidylinositol - PDZ PSD95/discslarge/ZO-1 - PI phosphoinositide - PIP2 phosphatidylinositol 4,5-bisphosphate - TCR T-cell receptor |
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Keywords: | Membrane raft Signal transduction Sphingolipid Cholesterol Oligomerisation |
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