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http://purl.uniprot.org/citations/16731528http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16731528http://www.w3.org/2000/01/rdf-schema#comment"Loss-of-function mutations in DJ-1 cause a subset of familial Parkinson disease (PD). However, the mechanism underlying the selective vulnerability in dopaminergic pathway due to the inactivation of DJ-1 is unclear. Previously, we have reported that DJ-1 is a neuroprotective transcriptional co-activator interacting with the transcriptional co-repressor pyrimidine tract-binding protein-associated splicing factor (PSF). Here we show that DJ-1 and PSF bind and regulate the human tyrosine hydroxylase (TH) promoter. Inactivation of DJ-1 by small interference RNA (siRNA) results in decreased TH expression and l-DOPA production in human dopaminergic cell lines. Consistent with its role as a transcriptional regulator, DJ-1 specifically suppresses the global SUMO-1 modification. High molecular weight sumoylated protein species, including PSF, accumulate in the lymphoblast cells from the patients carrying pathogenic DJ-1 mutations. DJ-1 elevates the TH expression by inhibiting the sumoylation of PSF and preventing its sumoylation-dependent recruitment of histone deacetylase 1. Furthermore, siRNA silencing of DJ-1 decreases the acetylation of TH promoter-bound histones, and histone deacetylase inhibitors restore the DJ-1 siRNA-induced repression of TH. Therefore, our results suggest DJ-1 as a regulator of protein sumoylation and directly link the loss of DJ-1 expression and transcriptional dysfunction to impaired dopamine synthesis."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m601935200"xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Kim C.Y."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Zhong N."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Squitieri F."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Rizzu P."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Heutink P."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Porter D.R."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Pothos E.N."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/author"Geula C."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/pages"20940-20948"xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/title"DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor."xsd:string
http://purl.uniprot.org/citations/16731528http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16731528http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16731528
http://purl.uniprot.org/citations/16731528http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16731528
http://purl.uniprot.org/uniprot/Q13547#attribution-BD49CB908D5CD3928B25DF43E8F1E2A0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528
http://purl.uniprot.org/uniprot/Q99497#attribution-88D7FF6C33245F645DA2361E8AAE6190http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528
http://purl.uniprot.org/uniprot/Q99497#attribution-BD49CB908D5CD3928B25DF43E8F1E2A0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528
http://purl.uniprot.org/uniprot/Q99497#attribution-E8F556F27221A81DA9CE79E587CD7DF0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528
http://purl.uniprot.org/uniprot/P23246#attribution-BD49CB908D5CD3928B25DF43E8F1E2A0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528
http://purl.uniprot.org/uniprot/P23246#attribution-E8F556F27221A81DA9CE79E587CD7DF0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16731528