http://purl.uniprot.org/citations/20212317 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20212317 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20212317 | http://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/20212317 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.200909008"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.200909008"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Mukhopadhyay D."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Mukhopadhyay D."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Arnaoutov A."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Arnaoutov A."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Dasso M."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/author | "Dasso M."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/name | "J. Cell Biol."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/pages | "681-692"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/pages | "681-692"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/title | "The SUMO protease SENP6 is essential for inner kinetochore assembly."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/title | "The SUMO protease SENP6 is essential for inner kinetochore assembly."xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/volume | "188"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://purl.uniprot.org/core/volume | "188"xsd:string |
http://purl.uniprot.org/citations/20212317 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20212317 |
http://purl.uniprot.org/citations/20212317 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20212317 |
http://purl.uniprot.org/citations/20212317 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20212317 |
http://purl.uniprot.org/citations/20212317 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20212317 |