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Article

Noncovalent interactions with SUMO and ubiquitin orchestrate distinct functions of the SLX4 complex in genome maintenance.

Molecular cell - 8 Jan 2015

Ouyang Jian, Garner Elizabeth, Hallet Alexander, Nguyen Hai Dang, Rickman Kimberly A, Gill Grace, Smogorzewska Agata, Zou Lee

Abstract excerpt

SLX4, a coordinator of multiple DNA structure-specific endonucleases, is important for several DNA repair pathways. Noncovalent interactions of SLX4 with ubiquitin are required for localizing SLX4 to DNA interstrand crosslinks (ICLs), yet how SLX4 is targeted to other functional contexts remains unclear. Here, we show that SLX4 binds SUMO-2/3 chains via SUMO-interacting motifs (SIMs). The SIMs of SLX4 are...

Topics

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Protein Interaction Domains and Motifs
Recombinases
Small Ubiquitin-Related Modifier Proteins
Telomere
Ubiquitin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ubiquitin-Conjugating Enzyme UBC9

Ubiquitin-Conjugating Enzymes

Source

Open in PubMed Open full text

Identifiers

PMID: 25533185
DOI: 10.1016/j.molcel.2014.11.015
PMCID: PMC4289429

Genes

SLX4
MDC1
MRE11
RAD50

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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