Proteomics

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Regulation of proteome by the proteasome upon ER stress


ABSTRACT: HeLa cells were with Tunicamycin or Thapsigargin for 8 hours in the presence or absence of MG132 or untreated. Cells were lysed by addition of HEPES 50 mM pH7.9 with 5% SDS. Proteins were precipitated with methanol/chloroforme and the proteins were resolubilized in 8 M Urea and digested with trypsin. The peptides were analyzed on a Thermofisher scientific Q Exactive HFX.

INSTRUMENT(S): Q Exactive

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

SUBMITTER: Bertrand Fabre  

PROVIDER: MSV000083736 | MassIVE | Tue Apr 30 04:36:00 BST 2019

REPOSITORIES: MassIVE

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Publications

Identification of proteins regulated by the proteasome following induction of endoplasmic reticulum stress.

Fabre Bertrand B   Livneh Ido I   Ziv Tamar T   Ciechanover Aaron A  

Biochemical and biophysical research communications 20190718 2


The endoplasmic reticulum (ER) is a major site for protein synthesis, folding and transport, lipid and steroid synthesis, regulating redox potential, as well as calcium storage. It therefore relies on delicate homeostasis, and perturbation of the ER function and induction of ER stress can lead to apoptosis. One cause of disruption of the ER homeostasis is the accumulation of misfolded proteins. To prevent this perturbation, the Endoplasmic Reticulum-Associated Degradation (ERAD) quality control  ...[more]

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