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http://purl.uniprot.org/citations/19074260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19074260http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19074260http://www.w3.org/2000/01/rdf-schema#comment"Autophagy is responsible for nonspecific, bulk degradation of cytoplasmic components. Recent work has revealed also that there is specific, autophagic degradation of polyubiquitinated protein aggregates, whose buildup occurs during neurodegenerative disease. Here, we report that simple mono-ubiquitination of normally long-lived cytoplasmic substrates is sufficient to target these substrates for autophagic degradation in mammalian cells. That is, upon their ubiquitination, both small [i.e., red fluorescent protein (RFP)] and large (i.e., peroxisomes) substrates are efficiently targeted to autophagosomes and then degraded within lysosomes upon autophagosome-lysosome fusion. This targeting requires the ubiquitin-binding protein, p62, and is blocked by the Class III phosphatidylinositol 3-kinase (PI3K) inhibitor, 3-methyladenine (3-MA), or by depletion of the autophagy-related-12 (Atg12) protein homolog. Mammalian cells thus use a common pathway involving ubiquitin and p62 for targeting diverse types of substrates for autophagy."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0810611105"xsd:string
http://purl.uniprot.org/citations/19074260http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0810611105"xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Mullen R.T."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Mullen R.T."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Lippincott-Schwartz J."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Lippincott-Schwartz J."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Kim P.K."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Kim P.K."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Hailey D.W."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/author"Hailey D.W."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/pages"20567-20574"xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/pages"20567-20574"xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/title"Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/title"Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes."xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/19074260http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/19074260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19074260
http://purl.uniprot.org/citations/19074260http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19074260