Results

RDF/XMLNTriplesTurtleShow queryShare ▶
SubjectPredicateObject
http://purl.uniprot.org/citations/25755297http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25755297http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25755297http://www.w3.org/2000/01/rdf-schema#comment"Genotoxic agents can cause replication fork stalling in dividing cells because of DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant SUMO target proteins are known. To address this, we have purified and identified SUMO-2 target proteins regulated by replication stress in human cells. The developed methodology enabled single step purification of His10-SUMO-2 conjugates under denaturing conditions with high yield and high purity. Following statistical analysis on five biological replicates, a total of 566 SUMO-2 targets were identified. After 2 h of hydroxyurea treatment, 10 proteins were up-regulated for SUMOylation and two proteins were down-regulated for SUMOylation, whereas after 24 h, 35 proteins were up-regulated for SUMOylation, and 13 proteins were down-regulated for SUMOylation. A site-specific approach was used to map over 1000 SUMO-2 acceptor lysines in target proteins. The methodology is generic and is widely applicable in the ubiquitin field. A large subset of these identified proteins function in one network that consists of interacting replication factors, transcriptional regulators, DNA damage response factors including MDC1, ATR-interacting protein ATRIP, the Bloom syndrome protein and the BLM-binding partner RMI1, the crossover junction endonuclease EME1, BRCA1, and CHAF1A. Furthermore, centromeric proteins and signal transducers were dynamically regulated by SUMOylation upon replication stress. Our results uncover a comprehensive network of SUMO target proteins dealing with replication damage and provide a framework for detailed understanding of the role of SUMOylation to counteract replication stress. Ultimately, our study reveals how a post-translational modification is able to orchestrate a large variety of different proteins to integrate different nuclear processes with the aim of dealing with the induced DNA damage."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.org/dc/terms/identifier"doi:10.1074/mcp.o114.044792"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.org/dc/terms/identifier"doi:10.1074/mcp.o114.044792"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.org/dc/terms/identifier"doi:10.1074/mcp.O114.044792"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Hendriks I.A."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Olsen J.V."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Vertegaal A.C."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Vertegaal A.C."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Xiao Z."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Xiao Z."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Chang J.G."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Chang J.G."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Sigurdsson J.O."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Sigurdsson J.O."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/author"Sigurethsson J.O."xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/name"Mol. Cell. Proteomics"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/name"Mol. Cell. Proteomics"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/pages"1419-1434"xsd:string
http://purl.uniprot.org/citations/25755297http://purl.uniprot.org/core/pages"1419-1434"xsd:string
▶