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PXD008529

PXD008529 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleChemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides
DescriptionThe 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.
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:13:37.528.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterTimothy Bergmann
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListmonohydroxylated residue; acetylated residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02017-12-21 03:01:32ID requested
12018-02-16 02:26:53announced
22018-02-17 00:30:23announcedUpdated project metadata.
32019-02-26 07:59:50announcedUpdated project metadata.
42024-10-22 04:13:38announced2024-10-22: 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 affiliationInstitute for research in biomedicine
contact emailmaurizio.molinari@irb.usi.ch
lab head
Timothy Bergmann
contact affiliationIRB
contact emailtimothy.bergmann@irb.usi.ch
dataset submitter
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Dataset FTP location
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PRIDE project URI
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