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http://purl.uniprot.org/citations/35732631http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35732631http://www.w3.org/2000/01/rdf-schema#comment"As a main regulator of cellular responses to hypoxia, the protein stability of hypoxia-inducible factor (HIF)-1α is strictly controlled by oxygen tension dependent of PHDs-catalyzed protein hydroxylation and pVHL complex-mediated proteasomal degradation. Whether HIF-1α protein stability as well as its activity can be further regulated under hypoxia is not well understood. In this study, we found that OTUB1 augments hypoxia signaling independent of PHDs/VHL and FIH. OTUB1 binds to HIF-1α and depletion of OTUB1 reduces endogenous HIF-1α protein under hypoxia. In addition, OTUB1 inhibits K48-linked polyubiquitination of HIF-1α via its non-canonical inhibition of ubiquitination activity. Furthermore, OTUB1 promotes hypoxia-induced glycolytic reprogramming for cellular metabolic adaptation. These findings define a novel regulation of HIF-1α under hypoxia and demonstrate that OTUB1-mediated HIF-1α stabilization positively regulates HIF-1α transcriptional activity and benefits cellular hypoxia adaptation."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.org/dc/terms/identifier"doi:10.1038/s41419-022-05008-z"xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Cai X."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Jia S."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Sun X."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Tang J."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Deng H."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Xiao W."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Zhu C."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Rong F."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/author"Ouyang G."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/name"Cell Death Dis"xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/pages"560"xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/title"OTUB1 augments hypoxia signaling via its non-canonical ubiquitination inhibition of HIF-1alpha during hypoxia adaptation."xsd:string
http://purl.uniprot.org/citations/35732631http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/35732631http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35732631
http://purl.uniprot.org/citations/35732631http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35732631
http://purl.uniprot.org/uniprot/#_D0VY79-mappedCitation-35732631http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35732631
http://purl.uniprot.org/uniprot/#_B2R617-mappedCitation-35732631http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35732631