Dataset Information

Mass Spectometry Analysis of Inhibition of SOD2-mediated protein degradation

ABSTRACT: Peptide samples were analysed by a shot-gun approach as described recently (Stieglitz et al., 2022). Raw MS data were processed using Max Quant (version 2.0, Cox and Mann 2008), Perseus software (version 2.0.6.0)(Tyanova et al.,2016), and human entries of uniprot DB. Proteins were stated identified by a false discovery rate of 0.01 on protein and peptide level.

INSTRUMENT(S): Orbitrap Exploris 240

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

SUBMITTER: PD Dr. Laura Hinze

PROVIDER: MSV000094325 | MassIVE | Fri Mar 15 05:29:00 GMT 2024

REPOSITORIES: MassIVE

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Publications

SOD2 is a regulator of proteasomal degradation promoting an adaptive cellular starvation response.

Ibrahim Nurul Khalida NK Schreek Sabine S Cinar Buesra B Stasche Anna Sophie AS Lee Su Hyun SH Zeug Andre A Dolgner Tim T Niessen Julia J Ponimaskin Evgeni E Shcherbata Halyna H Fehlhaber Beate B Bourquin Jean-Pierre JP Bornhauser Beat B Stanulla Martin M Pich Andreas A Gutierrez Alejandro A Hinze Laura L

Cell reports 20250324 4

Adaptation to changes in amino acid availability is crucial for cellular homeostasis, which requires an intricate orchestration of involved pathways. Some cancer cells can maintain cellular fitness upon amino acid shortage, which has a poorly understood mechanistic basis. Leveraging a genome-wide CRISPR-Cas9 screen, we find that superoxide dismutase 2 (SOD2) has a previously unrecognized dismutase-independent function. We demonstrate that SOD2 regulates global proteasomal protein degradation and ...[more]

PMID: 40131931

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