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http://purl.uniprot.org/citations/23382219http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23382219http://www.w3.org/2000/01/rdf-schema#comment"Transit of proteins through the endosomal organelle following endocytosis is critical for regulating the homeostasis of cell-surface proteins and controlling signal transduction pathways. However, the mechanisms that control these membrane-transport processes are poorly understood. The Phox-homology (PX) domain-containing proteins sorting nexin (SNX) 17, SNX27, and SNX31 have emerged recently as key regulators of endosomal recycling and bind conserved Asn-Pro-Xaa-Tyr-sorting signals in transmembrane cargos via an atypical band, 4.1/ezrin/radixin/moesin (FERM) domain. Here we present the crystal structure of the SNX17 FERM domain bound to the sorting motif of the P-selectin adhesion protein, revealing both the architecture of the atypical FERM domain and the molecular basis for recognition of these essential sorting sequences. We further show that the PX-FERM proteins share a promiscuous ability to bind a wide array of putative cargo molecules, including receptor tyrosine kinases, and propose a model for their coordinated molecular interactions with membrane, cargo, and regulatory proteins."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1216229110"xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Ghai R."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Liu H."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Teasdale R.D."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Collins B.M."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Li S.S."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Bugarcic A."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Skeldal S."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Norwood S.J."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/author"Coulson E.J."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/pages"E643-52"xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/title"Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins."xsd:string
http://purl.uniprot.org/citations/23382219http://purl.uniprot.org/core/volume"110"xsd:string
http://purl.uniprot.org/citations/23382219http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23382219
http://purl.uniprot.org/citations/23382219http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23382219
http://purl.uniprot.org/uniprot/P16066#attribution-6382EC52F66F3037AB93E6E041E6140Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219
http://purl.uniprot.org/uniprot/P18293#attribution-EB1255A01ABBCD2D2A67798D42DE4854http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219
http://purl.uniprot.org/uniprot/P12023#attribution-EB1255A01ABBCD2D2A67798D42DE4854http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219
http://purl.uniprot.org/uniprot/P05067#attribution-6382EC52F66F3037AB93E6E041E6140Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219
http://purl.uniprot.org/uniprot/Q8WXG9#attribution-6382EC52F66F3037AB93E6E041E6140Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219
http://purl.uniprot.org/uniprot/Q8VHN7#attribution-EB1255A01ABBCD2D2A67798D42DE4854http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23382219