| http://purl.uniprot.org/citations/17600709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17600709 | http://www.w3.org/2000/01/rdf-schema#comment | "Endocytosis has a crucial role in many cellular processes. The best-characterized mechanism for endocytosis involves clathrin-coated pits [1], but evidence has accumulated for additional endocytic pathways in mammalian cells [2]. One such pathway involves caveolae, plasma-membrane invaginations defined by caveolin proteins. Plasma-membrane microdomains referred to as lipid rafts have also been associated with clathrin-independent endocytosis by biochemical and pharmacological criteria [3]. The mechanisms, however, of nonclathrin, noncaveolin endocytosis are not clear [4, 5]. Here we show that coassembly of two similar membrane proteins, flotillin1 and flotillin2 [6-8], is sufficient to generate de novo membrane microdomains with some of the predicted properties of lipid rafts [9]. These microdomains are distinct from caveolin1-positive caveolae, are dynamic, and bud into the cell. Coassembly of flotillin1 and flotillin2 into microdomains induces membrane curvature, the formation of plasma-membrane invaginations morphologically similar to caveolae, and the accumulation of intracellular vesicles. We propose that flotillin proteins are defining structural components of the machinery that mediates a clathrin-independent endocytic pathway. Key attributes of this machinery are the dependence on coassembly of both flotillins and the inference that flotillin microdomains can exist in either flat or invaginated states."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cub.2007.05.078"xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Bright N.A."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Riento K."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Nichols B.J."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Frick M."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Bray A."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/author | "Merrified C."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/name | "Curr Biol"xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/pages | "1151-1156"xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/title | "Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding."xsd:string |
| http://purl.uniprot.org/citations/17600709 | http://purl.uniprot.org/core/volume | "17"xsd:string |
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