Proteomics

Dataset Information

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Cho_NFATC2IP_timsTOFPro2_P124_VS15


ABSTRACT: This dataset consists of 4 raw MS files and associated peak lists and results files, acquired on a Bruker timsTOF Pro 2 operated in Data Dependent Acquisition mode. Samples were generated by Tiffany Cho. Affinity purification was performed by Tiffany Cho and Laura McGary. Mass spectrometry acquisition was performed by Laura McGary. Analysis was performed by Tiffany Cho, Laura McGary, Cassandra Wong, and Daniel Durocher. The files are associated with a manuscript submitted for publication by Tiffany Cho et al. The main goal of this paper was to identify mechanisms required for the essential function of SUMO. This dataset showed no difference in differentially SUMOylated proteins upon knockout of NFATC2IP compared to WT. Daniel Durocher is the corresponding author of the manuscript (durocher@lunenfeld.ca); Karen Colwill should be contacted for questions on this dataset (colwill@lunenfeld.ca) This submission is associated with 2 Supplementary Files (in addition to this README file) Table 1 describes the composition of this dataset Table 2 lists all the peptide identification evidence

INSTRUMENT(S): timsTOF Pro 2

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Karen Colwill  

PROVIDER: MSV000094236 | MassIVE | Tue Mar 05 06:27:00 GMT 2024

SECONDARY ACCESSION(S): PXD050361

REPOSITORIES: MassIVE

Dataset's files

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Publications

NFATC2IP is a mediator of SUMO-dependent genome integrity.

Cho Tiffany T   Hoeg Lisa L   Setiaputra Dheva D   Durocher Daniel D  

Genes & development 20240417 5-6


The post-translational modification of proteins by SUMO is crucial for cellular viability and mammalian development in part due to the contribution of SUMOylation to genome duplication and repair. To investigate the mechanisms underpinning the essential function of SUMO, we undertook a genome-scale CRISPR/Cas9 screen probing the response to SUMOylation inhibition. This effort identified 130 genes whose disruption reduces or enhances the toxicity of TAK-981, a clinical-stage inhibitor of the SUMO  ...[more]

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