PXD008529 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides |
Description | The stress sensors ATF6, IRE1 and PERK monitor deviations from homeostatic conditions in the endoplasmic reticulum (ER), a protein biogenesis compartment of eukaryotic cells. Their activation elicits unfolded protein responses (UPR) to re-establish proteostasis. UPR have been extensively investigated in cells exposed to chemicals that activate ER stress sensors by perturbing calcium, sugars or redox homeostasis. Cell responses to variations in luminal load with unfolded proteins are, in contrast, poorly characterized. Here, we compared gene and protein expression profiles in cells challenged with ER stress-inducing drugs or expressing model polypeptides. Drugs titration to limit up-regulation of the endogenous ER stress reporters BiP/HSPA5 and HERP/HERPUD1 to levels comparable to luminal accumulation of unfolded proteins substantially reduced the amplitude of transcriptional and translational responses. Nevertheless, these remained pleiotropic and failed to recapitulate responses to ER load with unfolded proteins, which induced a limited subset of genes participating in a chaperone complex that binds unfolded chains. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:13:37.528.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Timothy Bergmann |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; acetylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-12-21 03:01:32 | ID requested | |
1 | 2018-02-16 02:26:53 | announced | |
2 | 2018-02-17 00:30:23 | announced | Updated project metadata. |
3 | 2019-02-26 07:59:50 | announced | Updated project metadata. |
⏵ 4 | 2024-10-22 04:13:38 | announced | 2024-10-22: Updated project metadata. |
Publication List
Bergmann TJ, Fregno I, Fumagalli F, Rinaldi A, Bertoni F, Boersema PJ, Picotti P, Molinari M, Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides. J Biol Chem, 293(15):5600-5612(2018) [pubmed] |
10.1074/jbc.ra117.001484; |
Keyword List
curator keyword: Biological |
submitter keyword: proteomics, endoplasmic reticulum stress (ER stress),endoplasmic reticulum (ER), transcriptomics, proteostasis, unfolded protein response (UPR) |
Contact List
Maurizio Molinari |
contact affiliation | Institute for research in biomedicine |
contact email | maurizio.molinari@irb.usi.ch |
lab head | |
Timothy Bergmann |
contact affiliation | IRB |
contact email | timothy.bergmann@irb.usi.ch |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD008529
- Label: PRIDE project
- Name: Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides