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http://purl.uniprot.org/citations/24637324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24637324http://www.w3.org/2000/01/rdf-schema#comment"The promyelocytic leukemia (PML) protein organizes PML nuclear bodies (NBs), which are stress-responsive domains where many partner proteins accumulate. Here, we clarify the basis for NB formation and identify stress-induced partner sumoylation as the primary NB function. NB nucleation does not rely primarily on intermolecular interactions between the PML SUMO-interacting motif (SIM) and SUMO, but instead results from oxidation-mediated PML multimerization. Oxidized PML spherical meshes recruit UBC9, which enhances PML sumoylation, allow partner recruitment through SIM interactions, and ultimately enhance partner sumoylation. Intermolecular SUMO-SIM interactions then enforce partner sequestration within the NB inner core. Accordingly, oxidative stress enhances NB formation and global sumoylation in vivo. Some NB-associated sumoylated partners also become polyubiquitinated by RNF4, precipitating their proteasomal degradation. As several partners are protein-modifying enzymes, NBs could act as sensors that facilitate and confer oxidative stress sensitivity not only to sumoylation but also to other post-translational modifications, thereby explaining alterations of stress response upon PML or NB loss."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201305148"xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"de The H."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Sahin U."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Setterblad N."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Jeanne M."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Jollivet F."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Niwa-Kawakita M."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Lallemand-Breitenbach V."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Berthier C."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Ferhi O."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Benhenda S."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/author"Faklaris O."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/pages"931-945"xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/title"Oxidative stress-induced assembly of PML nuclear bodies controls sumoylation of partner proteins."xsd:string
http://purl.uniprot.org/citations/24637324http://purl.uniprot.org/core/volume"204"xsd:string
http://purl.uniprot.org/citations/24637324http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24637324
http://purl.uniprot.org/citations/24637324http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24637324
http://purl.uniprot.org/uniprot/#_A0A068EW80-mappedCitation-24637324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24637324
http://purl.uniprot.org/uniprot/#_D3YXR5-mappedCitation-24637324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24637324
http://purl.uniprot.org/uniprot/#_F6XUT1-mappedCitation-24637324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24637324
http://purl.uniprot.org/uniprot/#_D3Z2V0-mappedCitation-24637324http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24637324