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http://purl.uniprot.org/citations/32073997http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32073997http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32073997http://www.w3.org/2000/01/rdf-schema#comment"The heterotetrameric adaptor protein complex 4 (AP-4) is a component of a protein coat associated with the trans-Golgi network (TGN). Mutations in AP-4 subunits cause a complicated form of autosomal-recessive hereditary spastic paraplegia termed AP-4-deficiency syndrome. Recent studies showed that AP-4 mediates export of the transmembrane autophagy protein ATG9A from the TGN to preautophagosomal structures. To identify additional proteins that cooperate with AP-4 in ATG9A trafficking, we performed affinity purification-mass spectrometry followed by validation of the hits by biochemical and functional analyses. This approach resulted in the identification of the fused toes homolog-Hook-FHIP (FHF) complex as a novel AP-4 accessory factor. We found that the AP-4-FHF interaction is mediated by direct binding of the AP-4 μ4 subunit to coiled-coil domains in the Hook1 and Hook2 subunits of FHF. Knockdown of FHF subunits resulted in dispersal of AP-4 and ATG9A from the perinuclear region of the cell, consistent with the previously demonstrated role of the FHF complex in coupling organelles to the microtubule (MT) retrograde motor dynein-dynactin. These findings thus uncover an additional mechanism for the distribution of ATG9A within cells and provide further evidence for a role of protein coats in coupling transport vesicles to MT motors."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e19-11-0658"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e19-11-0658"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Ren X."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Ren X."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Bonifacino J.S."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Bonifacino J.S."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Mattera R."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Mattera R."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Williamson C.D."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/author"Williamson C.D."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/pages"963-979"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/pages"963-979"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/title"The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/title"The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A."xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/32073997http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/32073997http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32073997
http://purl.uniprot.org/citations/32073997http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32073997