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ProteomicsSLX4 and SLX4IP TAP-MS - SLX4IP acts with SLX4 and XPF-ERCC1 to promote interstrand crosslink repair
Interstrand crosslinks (ICLs) are highly toxic DNA lesions, which are repaired via a complex process that requires the coordination of several DNA repair pathways. Defects in ICL repair result in Fanconi anemia (FA), which is diagnosed with bone marrow failure, development abnormalities and high inc...
ORGANISM(S): Homo sapiens (Human) 
2019-09-13 | PXD012521 | Pride
Sfb Slx4 Tap-ms Slx4ip 
ProteomicsSearching for new members of the SLX4 complex and for SLX4-complex members that are SUMOylated in vitro
The project was initially aimed at identifying new members of the SLX4 complex as well as members of the complex that are SUMOylated in vitro. The project was also aimed at assessing whether SUMOylation may change the compositon of the complex by reducing complex association of SUMOylated partners. ...
ORGANISM(S): Homo sapiens (Human) 
2020-03-05 | PXD012425 | Pride
Slx4 scaffold Protein sumoylation Interactome 
ProteomicsSearching for binding partners of the SLX4 577-795 region and assessing the impact of the SLX4 D614G and L618P cancer patient-derived mutations on their association with SLX4
The project was aimed at identifying new binding partners of SLX4 that associate with a region spanning the conserved amphipathic helix of SLX4 and the downstream BTB domain. It was also aimed at assessing which of those partners might have their association with SLX4 abrogated by the cancer patient...
ORGANISM(S): Homo sapiens (Human) 
2020-03-05 | PXD012426 | Pride
Slx4 scaffold Protein-protein binding domain Cancer associated mutations Interactome 
ProteomicsAprosoff_SLX4_APMS_P131_VS12_6600
This dataset consists of 15 raw MS files and associated peak lists and results files, acquired on AB Sciex TripleTOF 6600 mass spectrometer operated in Data Dependent Acquisition mode. Samples were generated by Camila Aprosoff. FLAG-AP and Mass spectrometry acquisition was performed by Zhen-Yuan Li...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000090314 | MassIVE
UnknownIdentification and characterization of MUS81 point mutations that abolish interaction with the SLX4 scaffold protein.
Not available
S-EPMC4251979 | biostudies-literature
UnknownDimerization of SLX4 contributes to functioning of the SLX4-nuclease complex.
Not available
S-EPMC4889959 | biostudies-literature
UnknownTermination of Replication Stress Signaling via Concerted Action of the Slx4 Scaffold and the PP4 Phosphatase.
Not available
S-EPMC4649662 | biostudies-literature
ProteomicsHA-mSLX4 wild type and SIMdependent interactors
SUMOylation is known to play important roles in the DNA damage response, however, a role for SUMOylation in interstrand crosslink repair remains enigmatic. We report on the regulation of the SLX4 nuclease scaffold protein by SUMOylation. SLX4 contains three SUMO-Interaction Motifs (SIMs). Mutating ...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2015-03-02 | PXD001681 | Pride
Dna repair Slx4 Fanconi anemia Sumo Ubiquitin 
OtherSUMOylation 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 ...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310007055 | GPMDB
Resource Reanalysis 
UnknownSLX4 dampens MutSα-dependent mismatch repair.
Not available
S-EPMC8934664 | biostudies-literature
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