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http://purl.uniprot.org/citations/27621083http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27621083http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27621083http://www.w3.org/2000/01/rdf-schema#comment"USP21 is a centrosome-associated deubiquitylase (DUB) that has been implicated in the formation of primary cilia - crucial organelles for the regulation of the Hedgehog (Hh) signaling pathway in vertebrates. Here, we identify KCTD6 - a cullin-3 E3-ligase substrate adapter that has been previously linked to Hh signaling - as well as Gli1, the key transcription factor responsible for Hh signal amplification, as new interacting partners of USP21. We identify a cryptic structured protein interaction domain in KCTD6, which is predicted to have a similar fold to Smr domains. Importantly, we show that both depletion and overexpression of catalytically active USP21 suppress Gli1-dependent transcription. Gli proteins are negatively regulated through protein kinase A (PKA)-dependent phosphorylation. We provide evidence that USP21 recruits and stabilises Gli1 at the centrosome where it promotes its phosphorylation by PKA. By revealing an intriguing functional pairing between a spatially restricted deubiquitylase and a kinase, our study highlights the centrosome as an important hub for signal coordination."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.org/dc/terms/identifier"doi:10.1242/jcs.188516"xsd:string
http://purl.uniprot.org/citations/27621083http://purl.org/dc/terms/identifier"doi:10.1242/jcs.188516"xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Rigden D.J."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Rigden D.J."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Urbe S."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Urbe S."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"De Smaele E."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"De Smaele E."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Clague M.J."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Clague M.J."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Cucchi D."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Cucchi D."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Bertsoulaki E."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Bertsoulaki E."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Heride C."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/author"Heride C."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/pages"4001-4013"xsd:string
http://purl.uniprot.org/citations/27621083http://purl.uniprot.org/core/pages"4001-4013"xsd:string