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Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex.

Abstract：

:In contrast to our extensive knowledge on covalent small ubiquitin-like modifier (SUMO) target proteins, we are limited in our understanding of non-covalent SUMO-binding proteins. We identify interactors of different SUMO isoforms-monomeric SUMO1, monomeric SUMO2, or linear trimeric SUMO2 chains-using a mass spectrometry-based proteomics approach. We identify 379 proteins that bind to different SUMO isoforms, mainly in a preferential manner. Interestingly, XRCC4 is the only DNA repair protein in our screen with a preference for SUMO2 trimers over mono-SUMO2, as well as the only protein in our screen that belongs to the non-homologous end joining (NHEJ) DNA double-strand break repair pathway. A SUMO interaction motif (SIM) in XRCC4 regulates its recruitment to sites of DNA damage and phosphorylation of S320 by DNA-PKcs. Our data highlight the importance of non-covalent and covalent sumoylation for DNA double-strand break repair via the NHEJ pathway and provide a resource of SUMO isoform interactors.

journal_name

Cell Rep

journal_title

Cell reports

authors

González-Prieto R,Eifler-Olivi K,Claessens LA,Willemstein E,Xiao Z,Talavera Ormeno CMP,Ovaa H,Ulrich HD,Vertegaal ACO

doi

10.1016/j.celrep.2021.108691

subject

Has Abstract

pub_date

2021-01-26 00:00:00

pages

108691

issue

4

issn

2211-1247

pii

S2211-1247(21)00004-8

journal_volume

34

pub_type

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