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http://purl.uniprot.org/citations/20889974http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20889974http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20889974http://www.w3.org/2000/01/rdf-schema#comment"Parkin is an E3 ubiquitin ligase that mediates the ubiquitination of protein substrates. The mutations in the parkin gene can lead to a loss of function of parkin and cause autosomal recessive juvenile onset parkinsonism. Recently, parkin was reported to be involved in the regulation of mitophagy. Here, we identify the Bcl-2, an anti-apoptotic and autophagy inhibitory protein, as a substrate for parkin. Parkin directly binds to Bcl-2 via its C terminus and mediates the mono-ubiquitination of Bcl-2, which increases the steady-state levels of Bcl-2. Overexpression of parkin, but not its ligase-deficient forms, decreases autophagy marker LC3 conversion, whereas knockdown of parkin increases LC3 II levels. In HeLa cells, a parkin-deficient cell line, knockdown of parkin does not change LC3 conversion. Moreover, overexpression of parkin enhances the interactions between Bcl-2 and Beclin 1. Our results provide evidence that parkin mono-ubiquitinates Bcl-2 and regulates autophagy via Bcl-2."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.101469"xsd:string
http://purl.uniprot.org/citations/20889974http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.101469"xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Chen D."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Chen D."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Gao F."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Gao F."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Zhu C."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/author"Zhu C."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/pages"38214-38223"xsd:string
http://purl.uniprot.org/citations/20889974http://purl.uniprot.org/core/pages"38214-38223"xsd:string