http://purl.uniprot.org/citations/22509284 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22509284 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/22509284 | http://www.w3.org/2000/01/rdf-schema#comment | "Increasing evidence has pointed to an important role of SUMOylation in cell cycle regulation, especially for M phase. In the current studies, we have obtained evidence through in vitro studies that the master M phase regulator CDK1/cyclin B kinase phosphorylates the SUMOylation machinery component Ubc9, leading to its enhanced SUMOylation activity. First, we show that CDK1/cyclin B, but not many other cell cycle kinases such as CDK2/cyclin E, ERK1, ERK2, PKA and JNK2/SAPK1, specifically enhances SUMOylation activity. Second, CDK1/cyclin B phosphorylates the SUMOylation machinery component Ubc9, but not SAE1/SAE2 or SUMO1. Third, CDK1/cyclin B-phosphorylated Ubc9 exhibits increased SUMOylation activity and elevated accumulation of the Ubc9-SUMO1 thioester conjugate. Fourth, CDK1/cyclin B enhances SUMOylation activity through phosphorylation of Ubc9 at serine 71. These studies demonstrate for the first time that the cell cycle-specific kinase CDK1/cyclin B phosphorylates a SUMOylation machinery component to increase its overall SUMOylation activity, suggesting that SUMOylation is part of the cell cycle program orchestrated by CDK1 through Ubc9."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0034250"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0034250"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Huang H."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Huang H."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Hwang J."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Hwang J."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Yang T."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Yang T."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Liu L.F."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Liu L.F."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Su Y.F."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/author | "Su Y.F."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/pages | "E34250"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/pages | "E34250"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/title | "Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/title | "Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity."xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/volume | "7"xsd:string |
http://purl.uniprot.org/citations/22509284 | http://purl.uniprot.org/core/volume | "7"xsd:string |