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http://purl.uniprot.org/citations/22652539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22652539http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22652539http://www.w3.org/2000/01/rdf-schema#comment"Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE). Atg8 functions in the formation of double-membrane autophagosomes, a central step in the well-conserved intracellular degradation pathway of macroautophagy (hereafter autophagy). Here we show that the deconjugation of Atg8-PE by the cysteine protease Atg4 plays dual roles in the formation of autophagosomes. During the early stage of autophagosome formation, deconjugation releases Atg8 from non-autophagosomal membranes to maintain a proper supply of Atg8. At a later stage, the release of Atg8 from intermediate autophagosomal membranes facilitates the maturation of these structures into fusion-capable autophagosomes. These results provide new insights into the functions of Atg8-PE and its deconjugation."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.org/dc/terms/identifier"doi:10.4161/auto.19652"xsd:string
http://purl.uniprot.org/citations/22652539http://purl.org/dc/terms/identifier"doi:10.4161/auto.19652"xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Liang Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Liang Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Xie Z."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Xie Z."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Klionsky D.J."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Klionsky D.J."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Hong B."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Hong B."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Wang H.Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Wang H.Y."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Ni T."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Ni T."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Zou S."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Zou S."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Yu Z.Q."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Yu Z.Q."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Jiang F.J."xsd:string
http://purl.uniprot.org/citations/22652539http://purl.uniprot.org/core/author"Jiang F.J."xsd:string