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Proteomics of HeLa cells starved and treated with YWF or leptomycin B

ABSTRACT: HeLa cells labeled with SILAC and were amino acids starved and treated with YWF, leptomycin B, MG132 or chloroquine. Cells were lysed with a 8M Urea buffer and proteins were reduced and alkylated. Equal amount of proteins of different labels were mixed and were digested with trypsin and resulting peptides were injected on a Q Exactive plus instrument. Raw data were analysed with MaxQuant with default settings.

INSTRUMENT(S): Q Exactive Plus

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

SUBMITTER: Bertrand Fabre

PROVIDER: MSV000092564 | MassIVE | Tue Aug 01 06:27:00 BST 2023

REPOSITORIES: MassIVE

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Publications

Regulation of nucleo-cytosolic 26S proteasome translocation by aromatic amino acids via mTOR is essential for cell survival under stress.

Livneh Ido I Cohen-Kaplan Victoria V Fabre Bertrand B Abramovitch Ifat I Lulu Chen C Nataraj Nishanth Belugali NB Lazar Ikrame I Ziv Tamar T Yarden Yosef Y Zohar Yaniv Y Gottlieb Eyal E Ciechanover Aaron A

Molecular cell 20230901 18

The proteasome is responsible for removal of ubiquitinated proteins. Although several aspects of its regulation (e.g., assembly, composition, and post-translational modifications) have been unraveled, studying its adaptive compartmentalization in response to stress is just starting to emerge. We found that following amino acid starvation, the proteasome is translocated from its large nuclear pool to the cytoplasm-a response regulated by newly identified mTOR-agonistic amino acids-Tyr, Trp, and P ...[more]

PMID: 37738964

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