Proteomics

Dataset Information

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HA-mSLX4 wild type and SIMdependent interactors

ABSTRACT: 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 all three SIMs abrogated the binding of SLX4 to SUMO-2 and covalent SLX4 SUMOylation. We attempt to identify which protein interaction are SIM dependent.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Román González-Prieto  

LAB HEAD: Alfred C O Vertegaal

PROVIDER: PXD001681 | Pride | 2015-03-02

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
MaxQuant_output.zip Other
RGP-HA-mSLX4-coIP-Control-1a.raw Raw
RGP-HA-mSLX4-coIP-Control-1b.raw Raw
RGP-HA-mSLX4-coIP-Control-1c.raw Raw
RGP-HA-mSLX4-coIP-Control-2a.raw Raw
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Publications

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  

EMBO reports 20150226 4

SUMOylation 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 dama  ...[more]