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http://purl.uniprot.org/citations/17010938http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17010938http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17010938http://www.w3.org/2000/01/rdf-schema#comment"RILP is emerging as a key regulator of late endocytic pathway by functioning as a downstream effector of activated Rab7 and Rab34, while ESCRT-I-->ESCRT-II-->ESCRT-III machinery acts in sorting proteins to the multivesicular body (MVB) initiated at the early/sorting endosome. We show here that the early machinery is integrated with the late machinery through a novel regulatory loop in which RILP interacts with VPS22 and VPS36 of ESCRT-II to mediate their membrane recruitment. The N-terminal and C-terminal half of RILP mediate interaction with VPS22 and VPS36, respectively. Overexpression of RILP leads to enlarged and clustered MVBs marked by lysobisphosphatidic acid (LBPA). In addition, RILP or its C-terminal fragment causes a retardation of sorting internalized EGF to the degradation route at the level of sorting endosomes marked by EEA1. We propose that RILP-->ESCRT-II serves as a regulatory/feedback loop to govern the coordination of early and late parts of the endocytic pathway."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.09.064"xsd:string
http://purl.uniprot.org/citations/17010938http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.09.064"xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/author"Hong W."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/author"Hong W."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/author"Wang T."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/pages"413-423"xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/pages"413-423"xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/title"RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/title"RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment."xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/volume"350"xsd:string
http://purl.uniprot.org/citations/17010938http://purl.uniprot.org/core/volume"350"xsd:string
http://purl.uniprot.org/citations/17010938http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17010938
http://purl.uniprot.org/citations/17010938http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17010938
http://purl.uniprot.org/citations/17010938http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17010938
http://purl.uniprot.org/citations/17010938http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17010938
http://purl.uniprot.org/uniprot/Q86VN1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17010938
http://purl.uniprot.org/uniprot/Q96H20http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17010938