| http://purl.uniprot.org/citations/11577110 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11577110 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11577110 | http://www.w3.org/2000/01/rdf-schema#comment | "Clathrin-mediated endocytosis is a major pathway for the internalization of macromolecules into the cytoplasm of eukaryotic cells. The principle coat components, clathrin and the AP-2 adaptor complex, assemble a polyhedral lattice at plasma membrane bud sites with the aid of several endocytic accessory proteins. Here, we show that huntingtin-interacting protein 1 (HIP1), a binding partner of huntingtin, copurifies with brain clathrin-coated vesicles and associates directly with both AP-2 and clathrin. The discrete interaction sequences within HIP1 that facilitate binding are analogous to motifs present in other accessory proteins, including AP180, amphiphysin, and epsin. Bound to a phosphoinositide-containing membrane surface via an epsin N-terminal homology (ENTH) domain, HIP1 associates with AP-2 to provide coincident clathrin-binding sites that together efficiently recruit clathrin to the bilayer. Our data implicate HIP1 in endocytosis, and the similar modular architecture and function of HIP1, epsin, and AP180 suggest a common role in lipid-regulated clathrin lattice biogenesis."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m108177200"xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m108177200"xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Mishra S.K."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Mishra S.K."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Traub L.M."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Traub L.M."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Brett T.J."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Brett T.J."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Ross T.S."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Ross T.S."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Agostinelli N.R."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Agostinelli N.R."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Mizukami I."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/author | "Mizukami I."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/pages | "46230-46236"xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/pages | "46230-46236"xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/title | "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins."xsd:string |
| http://purl.uniprot.org/citations/11577110 | http://purl.uniprot.org/core/title | "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role for endocytic accessory proteins."xsd:string |