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http://purl.uniprot.org/citations/21771882http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21771882http://www.w3.org/2000/01/rdf-schema#comment"Proteolytic systems and the aggresome pathway contribute to preventing accumulation of cytotoxic aggregation-prone proteins. Although polyubiquitylation is usually required for degradation or aggresome formation, several substrates are processed independently of ubiquitin through a poorly understood mechanism. Here, we found that p62/SQSTM1, a multifunctional adaptor protein, was involved in the selective autophagic clearance of a non-ubiquitylated substrate, namely an aggregation-prone isoform of STAT5A (STAT5A_ΔE18). By using a cell line that stably expressed STAT5A_ΔE18, we investigated the properties of its aggregation and degradation. We found that STAT5A_ΔE18 formed non-ubiquitylated aggresomes and/or aggregates by impairment of proteasome functioning or autophagy. Transport of these aggregates to the perinuclear region was inhibited by trichostatin A or tubacin, inhibitors of histone deacetylase (HDAC), indicating that the non-ubiquitylated aggregates of STAT5A_ΔE18 were sequestered into aggresomes in an HDAC6-dependent manner. Moreover, p62 was bound to STAT5A_ΔE18 through its PB1 domain, and the oligomerization of p62 was required for this interaction. In p62-knockdown experiments, we found that p62 was required for autophagic clearance of STAT5A_ΔE18 but not for its aggregate formation, suggesting that the binding of p62 to non-ubiquitylated substrates might trigger their autophagic clearance."xsd:string
http://purl.uniprot.org/citations/21771882http://purl.org/dc/terms/identifier"doi:10.1242/jcs.081232"xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/author"Watanabe Y."xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/author"Tanaka M."xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/pages"2692-2701"xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/title"p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate."xsd:string
http://purl.uniprot.org/citations/21771882http://purl.uniprot.org/core/volume"124"xsd:string
http://purl.uniprot.org/citations/21771882http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21771882
http://purl.uniprot.org/citations/21771882http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21771882
http://purl.uniprot.org/uniprot/#_B3FTN5-mappedCitation-21771882http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/#_B4DKT5-mappedCitation-21771882http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/#_F8W930-mappedCitation-21771882http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/#_Q9Y6M1-mappedCitation-21771882http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/F8W930http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/Q9Y6M1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/B3FTN5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21771882
http://purl.uniprot.org/uniprot/B4DKT5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21771882