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http://purl.uniprot.org/citations/20212317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20212317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20212317http://www.w3.org/2000/01/rdf-schema#comment"We have analyzed the mitotic function of SENP6, a small ubiquitin-like modifier (SUMO) protease that disassembles conjugated SUMO-2/3 chains. Cells lacking SENP6 showed defects in spindle assembly and metaphase chromosome congression. Analysis of kinetochore composition in these cells revealed that a subset of proteins became undetectable on inner kinetochores after SENP6 depletion, particularly the CENP-H/I/K complex, whereas other changes in kinetochore composition mimicked defects previously reported to result from CENP-H/I/K depletion. We further found that CENP-I is degraded through the action of RNF4, a ubiquitin ligase which targets polysumoylated proteins for proteasomal degradation, and that SENP6 stabilizes CENP-I by antagonizing RNF4. Together, these findings reveal a novel mechanism whereby the finely balanced activities of SENP6 and RNF4 control vertebrate kinetochore assembly through SUMO-targeted destabilization of inner plate components."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200909008"xsd:string
http://purl.uniprot.org/citations/20212317http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200909008"xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Mukhopadhyay D."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Mukhopadhyay D."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Arnaoutov A."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Arnaoutov A."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Dasso M."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/author"Dasso M."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/pages"681-692"xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/pages"681-692"xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/title"The SUMO protease SENP6 is essential for inner kinetochore assembly."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/title"The SUMO protease SENP6 is essential for inner kinetochore assembly."xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/volume"188"xsd:string
http://purl.uniprot.org/citations/20212317http://purl.uniprot.org/core/volume"188"xsd:string
http://purl.uniprot.org/citations/20212317http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20212317
http://purl.uniprot.org/citations/20212317http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20212317
http://purl.uniprot.org/citations/20212317http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20212317
http://purl.uniprot.org/citations/20212317http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20212317