SUMOylation and PARylation cooperate to recruit and stabilize SLX4 at DNA damage sites.

ABSTRACT: 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}}

INSTRUMENT(S): Instrument

ORGANISM(S): Homo_sapiens_viruses, Human_female

DISEASE(S): Not Available

SUBMITTER: Gonzalez-Prieto R, et al.  

PROVIDER: GPM32310007055 | GPMDB |

REPOSITORIES: GPMDB