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http://purl.uniprot.org/citations/12952949http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12952949http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12952949http://www.w3.org/2000/01/rdf-schema#comment"Sorting nexin 9 (SNX9) belongs to a family of proteins, the sorting nexins, that are characterized by the presence of a subclass of the phosphoinositide-binding phox domain. SNX9 has in its amino terminus a Src homology 3 domain and a region with predicted low complexity followed by a carboxyl-terminal part containing the phox domain. We previously found that SNX9 is one of the major proteins in hematopoietic cells that binds to the alpha and beta2-appendages of adaptor protein complex 2 (AP-2), a protein with a critical role in the formation of clathrin-coated vesicles at the plasma membrane. In the present study we show that clathrin and dynamin-2, two other essential molecules in the endocytic process, also interact with SNX9. We found that both AP-2 and clathrin bind to the low complexity region in SNX9 in a cooperative manner, whereas dynamin-2 binds to the Src homology 3 domain. In the cytosol, SNX9 is present in a 14.5 S complex containing dynamin-2 and an unidentified 41-kDa protein. In HeLa cells, SNX9 co-localized with both AP-2 and dynamin-2 at the plasma membrane or on vesicular structures derived from it but not with the early endosomal marker EEA1 or with AP-1. The results suggest that SNX9 may be recruited together with dynamin-2 and become co-assembled with AP-2 and clathrin at the plasma membrane. Overexpression in both K562 and HeLa cells of truncated forms of SNX9 interfered with the uptake of transferrin, consistent with a role of SNX9 in endocytosis."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m307334200"xsd:string
http://purl.uniprot.org/citations/12952949http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m307334200"xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/author"Carlsson S.R."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/author"Lundmark R."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/author"Lundmark R."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/pages"46772-46781"xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/pages"46772-46781"xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/title"Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/title"Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components."xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12952949http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12952949http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12952949
http://purl.uniprot.org/citations/12952949http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12952949
http://purl.uniprot.org/citations/12952949http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12952949
http://purl.uniprot.org/citations/12952949http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12952949
http://purl.uniprot.org/uniprot/Q9Y5X1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12952949
http://purl.uniprot.org/uniprot/Q9Y5X1#attribution-F5B5177E281E1F787D1D9C5E0263FDE0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12952949