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http://purl.uniprot.org/citations/22002062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22002062http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22002062http://www.w3.org/2000/01/rdf-schema#comment"The molecular mechanisms underlying protein turnover and enzyme regulation in the peroxisomal matrix remain largely unknown. Trypsin domain-containing 1 (Tysnd1) and peroxisomal Lon protease (PsLon) are newly identified peroxisomal matrix proteins that harbor both a serine protease-like domain and a peroxisome-targeting signal 1 (PTS1) sequence. Tysnd1 processes several PTS1-containing proteins and cleaves N-terminal presequences from PTS2-containing protein precursors. Here we report that knockdown of Tysnd1, but not PsLon, resulted in accumulation of endogenous β-oxidation enzymes in their premature form. The protease activity of Tysnd1 was inactivated by intermolecular self-conversion of the 60-kDa form to 15- and 45-kDa chains, which were preferentially degraded by PsLon. Peroxisomal β-oxidation of a very long fatty acid was significantly decreased by knockdown of Tysnd1 and partially lowered by PsLon knockdown. Taken together, these data suggest that Tysnd1 is a key regulator of the peroxisomal β-oxidation pathway via proteolytic processing of β-oxidation enzymes. The proteolytic activity of oligomeric Tysnd1 is in turn controlled by self-cleavage of Tysnd1 and degradation of Tysnd1 cleavage products by PsLon."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.285197"xsd:string
http://purl.uniprot.org/citations/22002062http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.285197"xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Fujiki Y."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Fujiki Y."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Okumoto K."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Okumoto K."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Kametani Y."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/author"Kametani Y."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/pages"44367-44379"xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/pages"44367-44379"xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/title"Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid beta-oxidation in peroxisomal matrix."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/title"Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid beta-oxidation in peroxisomal matrix."xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/22002062http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/22002062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22002062
http://purl.uniprot.org/citations/22002062http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22002062
http://purl.uniprot.org/citations/22002062http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22002062
http://purl.uniprot.org/citations/22002062http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22002062