PXD022924

PXD022924 is an original dataset announced via ProteomeXchange.

Title	Uncovering Global Non-Covalent SUMO Binder Networks Reveals that Sumoylation enhances XRCC4 activitythe stabilization of the classical Non Homologous End Joining complex.
Description	In contrast to our extensive knowledge on covalent SUMO target proteins, we are limited in our understanding of proteins that bind SUMO family members in a non-covalent manner. We have identified interactors of different SUMO isoforms: monomeric SUMO1, monomeric SUMO2 or linear trimeric SUMO2 chains, using a mass spectrometry-based proteomics approach. We identified 382 proteins that bind to different SUMO isoforms mainly in a preferential manner. Interestingly, XRCC4 was 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 functional SIM in XRCC4 regulated its recruitment to local sites of DNA damage and its phosphorylation in S320 by DNA-PKcs. Combined, our data highlight the importance of non-covalent and covalent sumoylation for DNA double-strand break repair via the NHEJ pathway and provides a resource of SUMO isoform interactors.
HostingRepository	PRIDE
AnnounceDate	2021-01-29
AnnouncementXML	Submission_2021-01-28_22:53:13.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Román González-Prieto
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2020-12-04 07:44:24	ID requested
⏵ 1	2021-01-28 22:53:14	announced

Gonz, á, lez-Prieto R, Eifler-Olivi K, Claessens LA, Willemstein E, Xiao Z, Talavera Ormeno CMP, Ovaa H, Ulrich HD, Vertegaal ACO, Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex. Cell Rep, 34(4):108691(2021) [pubmed]

submitter keyword: SUMO, Proteomics, Non Homologous End Joining, XRCC4

Alfred C.O. Vertegaal
contact affiliation	Cell and Chemical Biology LUMC Leiden The Netherlands
contact email	vertegaal@lumc.nl
lab head
Román González-Prieto
contact affiliation	Leiden University Medical Center (LUMC)
contact email	R.Gonzalez_Prieto@lumc.nl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD022924
     1. Label: PRIDE project
     2. Name: Uncovering Global Non-Covalent SUMO Binder Networks Reveals that Sumoylation enhances XRCC4 activitythe stabilization of the classical Non Homologous End Joining complex.