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http://purl.uniprot.org/citations/16516836http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16516836http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16516836http://www.w3.org/2000/01/rdf-schema#comment"Clathrin-associated sorting proteins (CLASPs) expand the repertoire of endocytic cargo sorted into clathrin-coated vesicles beyond the transmembrane proteins that bind physically to the AP-2 adaptor. LDL and GPCRs are internalized by ARH and beta-arrestin, respectively. We show that these two CLASPs bind selectively to the AP-2 beta2 appendage platform via an alpha-helical [DE](n)X(1-2)FXX[FL]XXXR motif, and that this motif also occurs and is functional in the epsins. In beta-arrestin, this motif maintains the endocytosis-incompetent state by binding back on the folded core of the protein in a beta strand conformation. Triggered via a beta-arrestin/GPCR interaction, the motif must be displaced and must undergo a strand to helix transition to enable the beta2 appendage binding that drives GPCR-beta-arrestin complexes into clathrin coats. Another interaction surface on the beta2 appendage sandwich is identified for proteins such as eps15 and clathrin, suggesting a mechanism by which clathrin displaces eps15 to lattice edges during assembly."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2006.01.016"xsd:string
http://purl.uniprot.org/citations/16516836http://purl.org/dc/terms/identifier"doi:10.1016/j.devcel.2006.01.016"xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Roth R."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Roth R."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Mishra S.K."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Mishra S.K."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Collins B.M."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Collins B.M."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Edeling M.A."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Edeling M.A."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Traub L.M."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Traub L.M."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Heuser J.E."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Heuser J.E."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Keyel P.A."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Keyel P.A."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Owen D.J."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Owen D.J."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Steinhauser A.L."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/author"Steinhauser A.L."xsd:string
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16516836http://purl.uniprot.org/core/date"2006"xsd:gYear