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http://purl.uniprot.org/citations/11517213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11517213http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11517213http://www.w3.org/2000/01/rdf-schema#comment"Polyglutamine expansion in huntingtin is the underlying mutation leading to neurodegeneration in Huntington disease. This mutation influences the interaction of huntingtin with different proteins, including huntingtin-interacting protein 1 (HIP1), in which affinity to bind to mutant huntingtin is profoundly reduced. Here we demonstrate that HIP1 colocalizes with markers of clathrin-mediated endocytosis in neuronal cells and is highly enriched on clathrin-coated vesicles (CCVs) purified from brain homogenates. HIP1 binds to the clathrin adaptor protein 2 (AP2) and the terminal domain of the clathrin heavy chain, predominantly through a small fragment encompassing amino acids 276-335. This region, which contains consensus clathrin- and AP2-binding sites, functions in conjunction with the coiled-coil domain to target HIP1 to CCVs. Expression of various HIP1 fragments leads to a potent block of clathrin-mediated endocytosis. Our findings demonstrate that HIP1 is a novel component of the endocytic machinery."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100401200"xsd:string
http://purl.uniprot.org/citations/11517213http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c100401200"xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Gan L."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Gan L."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"McPherson P.S."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Hayden M.R."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Hayden M.R."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Metzler M."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Metzler M."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Chopra V."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Chopra V."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Legendre-Guillemin V."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Legendre-Guillemin V."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Kwok A."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/author"Kwok A."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/pages"39271-39276"xsd:string
http://purl.uniprot.org/citations/11517213http://purl.uniprot.org/core/pages"39271-39276"xsd:string