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Please use this identifier to cite or link to this item: http://hdl.handle.net/2289/2727
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dc.contributor.authorSharma, Pranav-
dc.contributor.authorVarma, Rajat-
dc.contributor.authorSarasij, R.C.-
dc.contributor.authorKarine Gousset, Ira-
dc.contributor.authorKrishnamoorthy, G.-
dc.contributor.authorRao, Madan-
dc.contributor.authorMayor, Satyajit-
dc.date.accessioned2007-06-11T09:48:43Z-
dc.date.available2007-06-11T09:48:43Z-
dc.date.issued2004-02-
dc.identifier.citationCell, 2004, Vol.116, p577-589en
dc.identifier.issn0092-8674-
dc.identifier.urihttp://hdl.handle.net/2289/2727-
dc.descriptionRestricted Access.en
dc.description.abstractCholesterol and sphingolipid-enriched “rafts” have long been proposed as platforms for the sorting of specific membrane components including glycosyl-phosphatidylinositol-anchored proteins (GPI-APs), however, their existence and physical properties have been controversial. Here, we investigate the size of lipid-dependent organization of GPI-APs in live cells, using homo and hetero-FRET-based experiments, combined with theoretical modeling. These studies reveal an unexpected organization wherein cell surface GPI-APs are present as monomers and a smaller fraction (20%–40%) as nanoscale (<5 nm) cholesterol-sensitive clusters. These clusters are composed of at most four molecules and accommodate diverse GPI-AP species; crosslinking GPI-APs segregates them from preexisting GPI-AP clusters and prevents endocytosis of the crosslinked species via a GPI-AP-selective pinocytic pathway. In conjunction with an analysis of the statistical distribution of the clusters, these observations suggest a mechanism for functional lipid-dependent clustering of GPI-APs.en
dc.format.extent624577 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.publisherElsevier B.V.en
dc.relation.urihttp://dx.doi.org/10.1016/S0092-8674(04)00167-9en
dc.rights2004 Elsevier B.V.en
dc.titleNanoscale Organization of Multiple GPI-Anchored Proteins in Living Cell Membranesen
dc.typeArticleen
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