GPMDB00395OtherGonzalez-Prieto R, et al.InstrumentNot AvailableNot availableHomo_sapiens_viruses, Human_femaleA.C.O.Vertegaal@lumc.nl25722289Department of Molecular Cell Biology, Leiden University Medical Center, Leidenhttp://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007068http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007069http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007066http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007067http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007071http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007072http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007070http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007075http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007076http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007054http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007073http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007074http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007079http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007057http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007058http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007077http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007055http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007078http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007056http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007059http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007061http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007080http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007064http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007065http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007062http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007063Not availableGPMDBSUMOylation plays important roles in the DNA damage response. However, whether it is important for interstrand crosslink repair remains unknown. We report that the SLX4 nuclease scaffold protein is regulated by SUMOylation. We have identified three SUMO interaction motifs (SIMs) in SLX4, mutating all of which abrogated the binding of SLX4 to SUMO-2 and covalent SLX4 SUMOylation. An SLX4 mutant lacking functional SIMs is not recruited to PML nuclear bodies nor stabilized at laser-induced DNA damage sites. Additionally, we elucidated a novel role for PARylation in the recruitment of SLX4 to sites of DNA damage. Combined, our results uncover how SLX4 is regulated by post-translational modifications.SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.González-Prieto Román R,Cuijpers Sabine A G SA,Luijsterburg Martijn S MS,van Attikum Haico H,Vertegaal Alfred C O AC,González-Prieto Román R, Cuijpers Sabine A G SA, Luijsterburg Martijn S MS, van Attikum Haico H, Vertegaal Alfred C O ACDNA Injury, Genotoxic Stress, sumoylation, DNA Injuries, Injury, Genotoxic Stresses, SUMO-Conjugations, SUMO-protein conjugation, protein sumolation, FANCP, DNA Damages, Damage, Injuries, Damages, SUMO Conjugation, Stresses, Genotoxic, BTBD12, Sumoylations, Stress, MUS312, SUMO-Conjugation, DNA, DNA., small ubiquitin-related protein 1 conjugationsumoylation, data, Controlling, Rab interactor activity, multinuclear leukocyte, Genotoxic Stresses, SUMO-Conjugations, Smt3b, SUMO-protein conjugation, Smt3h2, Sentrin-2, DNA Damages, HSMT3, Damage, light amplification by the stimulated emission of radiation, Damages, Stresses, MYL, SUMO, Rab escort protein activity, Trim19, AI661194, Sumoylations, MUS312, TRIM19, DNA., SMT3 homolog 2, small ubiquitin-related protein 1 conjugation, SMT3 homolog 1, DNA Injury, Genotoxic Stress, DNA Injuries, Injury, reference sample, RNF71, ligand, 1200009E24Rik, protein sumolation, Ubiquitin-like protein SMT3B, FANCP, PP8675, SUMO-2, SUMO-3, Injuries, SUMO Conjugation, Genotoxic, Ubiquitin-like protein SMT3A, BTBD12, Smt3A, Smt3B, PML, Stress, polymorphonuclear leucocyte, SUMO-Conjugation, DNA, REP, ControlledDNA Injury, Genotoxic Stress, sumoylation, DNA Injuries, Injury, Genotoxic Stresses, SUMO-Conjugations, SUMO-protein conjugation, protein sumolation, FANCP, DNA Damages, Damage, Injuries, Damages, SUMO Conjugation, Stresses, Genotoxic, BTBD12, Sumoylations, Stress, MUS312, SUMO-Conjugation, DNA, DNA., small ubiquitin-related protein 1 conjugationsumoylation, DNA damage response, multinuclear leukocyte, Genotoxic Stresses, SUMO-Conjugations, Smt3b, SUMO-protein conjugation, Smt3h2, response to DNA damage stimulus, Sentrin-2, DNA Damages, HSMT3, Damage, results, light amplification by the stimulated emission of radiation, Damages, Stresses, Concept, MYL, SUMO, Trim19, Role Concept, Roles, AI661194, Sumoylations, MUS312, Role, Concepts, TRIM19, SMT3 homolog 2, small ubiquitin-related protein 1 conjugation, SMT3 homolog 1, DNA Injury, Genotoxic Stress, DNA Injuries, Injury, cellular DNA damage response, RNF71, ligand, 1200009E24Rik, protein sumolation, Ubiquitin-like protein SMT3B, FANCP, PP8675, SUMO-2, SUMO-3, Injuries, response to genotoxic stress, SUMO Conjugation, Genotoxic, Ubiquitin-like protein SMT3A, BTBD12, Smt3A, Smt3B, BTBD12., PML, Stress, Role Concepts, polymorphonuclear leucocyte, SUMO-Conjugation, DNA3905http://gpmdb.thegpm.org/~/dblist_gpmnum/gpmnum=GPM32310007055dbgap_ncbi~0patentfamilies~0rfam~0merops~0complex-portal~0uniprot~0wormbaseparasite~0embl-covid19~0reactome~0emdb~0wgs_masters~0ebiweb_resources~0opentargets_genetics~0biomodels_all~0ipd-mhc~0ebiweb_teams~0taxonomy~0genome_assembly~0sc-experiments~0ebiweb_people~0enzymeportal_enzymes~0ipd-nhkir~0cellosaurus~0pdbe~0chebi~0patentproteins~0interpro7~0uniref~0chembl~0pdbekb~0gpcrdb~0hgnc~0sc-genes~0intact~0rhea~0ebiweb_training~0alphafold~0imgt-hla~0patentnucleotides~0ensemblroot~0eva_studies~0non-coding~0europepmc~0pubmed~1identifiers_registry~0pdbechem~0hpa-covid19~0eva-variants-covid19~0biosamples~0gwas_catalog~0biotools~0tls_masters~0mesh~0coding~0sra~0opentargets~0efo~0embl-pathogen~0project~0pride~1human_diseases~0geo_datasets~0embl~0treefam~0uniparc~0ols~0dgva~0intenz~0go~0tsa_masters~0biosamples-covid19~0ebiweb_corporate~0omim~0lrg~0earlycause-molecular-sequences~0ipd-kir~0empiar~0rnacentral~0orcid_data_claims~0gpmdb~2lineage-covid19~0metagenomics~0pfam~0pride archive~1varsite~00Resource Reanalysis0.00.00.0120296113510178910.01.0falseSUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.Data from ProteomeXchange, PXD ID: PXD001681. File: RGP-HA-mSLX4-coIP-Control-1b.mzml. Published as part of EMBO Rep. 2015 Feb 26 . From the Abstract: {{i}} ... We report that the SLX4 nuclease scaffold protein is regulated by SUMOylation. We have identified three SUMO interaction motifs (SIMs) in SLX4, mutating all of which abrogated the binding of SLX4 to SUMO-2 and covalent SLX4 SUMOylation. An SLX4 mutant lacking functional SIMs is not recruited to PML nuclear bodies nor stabilized at laser-induced DNA damage sites ... {{/i}}2015-03-02GPM3231000705525722289PXD001681PXD001681