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http://purl.uniprot.org/citations/31006538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31006538http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31006538http://www.w3.org/2000/01/rdf-schema#comment"Certain proteins and organelles can be selectively degraded by autophagy. Typical substrates and receptors of selective autophagy have LC3-interacting regions (LIRs) that bind to autophagosomal LC3 and GABARAP family proteins. Here, we performed a differential interactome screen using wild-type LC3B and a LIR recognition-deficient mutant and identified TEX264 as a receptor for autophagic degradation of the endoplasmic reticulum (ER-phagy). TEX264 is an ER protein with a single transmembrane domain and a LIR motif. TEX264 interacts with LC3 and GABARAP family proteins more efficiently and is expressed more ubiquitously than previously known ER-phagy receptors. ER-phagy is profoundly blocked by deletion of TEX264 alone and almost completely by additional deletion of FAM134B and CCPG1. A long intrinsically disordered region of TEX264 is required for its ER-phagy receptor function to bridge the gap between the ER and autophagosomal membranes independently of its amino acid sequence. These results suggest that TEX264 is a major ER-phagy receptor."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2019.03.033"xsd:string
http://purl.uniprot.org/citations/31006538http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2019.03.033"xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Hatta T."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Hatta T."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Natsume T."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Natsume T."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Mizushima N."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Chino H."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/author"Chino H."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/title"Intrinsically disordered protein TEX264 mediates ER-phagy."xsd:string
http://purl.uniprot.org/citations/31006538http://purl.uniprot.org/core/title"Intrinsically disordered protein TEX264 mediates ER-phagy."xsd:string
http://purl.uniprot.org/citations/31006538http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31006538
http://purl.uniprot.org/citations/31006538http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31006538
http://purl.uniprot.org/citations/31006538http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31006538
http://purl.uniprot.org/citations/31006538http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31006538
http://purl.uniprot.org/uniprot/Q9GZQ8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/31006538
http://purl.uniprot.org/uniprot/O95166http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/31006538