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http://purl.uniprot.org/citations/25355947http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25355947http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25355947http://www.w3.org/2000/01/rdf-schema#comment"COMMD1 deficiency results in defective copper homeostasis, but the mechanism for this has remained elusive. Here we report that COMMD1 is directly linked to early endosomes through its interaction with a protein complex containing CCDC22, CCDC93, and C16orf62. This COMMD/CCDC22/CCDC93 (CCC) complex interacts with the multisubunit WASH complex, an evolutionarily conserved system, which is required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. Interactions between the WASH complex subunit FAM21, and the carboxyl-terminal ends of CCDC22 and CCDC93 are responsible for CCC complex recruitment to endosomes. We show that depletion of CCC complex components leads to lack of copper-dependent movement of the copper transporter ATP7A from endosomes, resulting in intracellular copper accumulation and modest alterations in copper homeostasis in humans with CCDC22 mutations. This work provides a mechanistic explanation for the role of COMMD1 in copper homeostasis and uncovers additional genes involved in the regulation of copper transporter recycling."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e14-06-1073"xsd:string
http://purl.uniprot.org/citations/25355947http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e14-06-1073"xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Deng Z."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Deng Z."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Kaufmann S.H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Kaufmann S.H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Zhang J.S."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Zhang J.S."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Dai H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Dai H."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Billadeau D.D."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Billadeau D.D."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Gomez T.S."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Gomez T.S."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"McGaughran J."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"McGaughran J."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Gecz J."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"Gecz J."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"van de Sluis B."xsd:string
http://purl.uniprot.org/citations/25355947http://purl.uniprot.org/core/author"van de Sluis B."xsd:string