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http://purl.uniprot.org/citations/30451685http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30451685http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30451685http://www.w3.org/2000/01/rdf-schema#comment"The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular β-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.org/dc/terms/identifier"doi:10.7554/elife.41237"xsd:string
http://purl.uniprot.org/citations/30451685http://purl.org/dc/terms/identifier"doi:10.7554/elife.41237"xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Wu J.Q."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Wu J.Q."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Noda N.N."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Noda N.N."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Liu X.M."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Liu X.M."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Nakatogawa H."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Nakatogawa H."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Du L.L."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Du L.L."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Coffman V.C."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Coffman V.C."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Du X.M."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Du X.M."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Yamasaki A."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/author"Yamasaki A."xsd:string
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30451685http://purl.uniprot.org/core/date"2018"xsd:gYear