RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11161217http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11161217http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11161217http://www.w3.org/2000/01/rdf-schema#comment"Endocytic proteins such as epsin, AP180, and Hip1R (Sla2p) share a conserved modular region termed the epsin NH2-terminal homology (ENTH) domain, which plays a crucial role in clathrin-mediated endocytosis through an unknown target. Here, we demonstrate a strong affinity of the ENTH domain for phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2]. With nuclear magnetic resonance analysis of the epsin ENTH domain, we determined that a cleft formed with positively charged residues contributed to phosphoinositide binding. Overexpression of a mutant, epsin Lys76 --> Ala76, with an ENTH domain defective in phosphoinositide binding, blocked epidermal growth factor internalization in COS-7 cells. Thus, interaction between the ENTH domain and PtdIns(4,5)P2 is essential for endocytosis mediated by clathrin-coated pits."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.org/dc/terms/identifier"doi:10.1126/science.291.5506.1047"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.org/dc/terms/identifier"doi:10.1126/science.291.5506.1047"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Itoh T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Itoh T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Yokoyama S."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Kigawa T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Kigawa T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Koshiba S."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Koshiba S."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Takenawa T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/author"Takenawa T."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/pages"1047-1051"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/pages"1047-1051"xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/title"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis."xsd:string
http://purl.uniprot.org/citations/11161217http://purl.uniprot.org/core/title"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis."xsd:string