PXD008529

PXD008529 is an original dataset announced via ProteomeXchange.

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

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.

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;

curator keyword: Biological

submitter keyword: proteomics, endoplasmic reticulum stress (ER stress),endoplasmic reticulum (ER), transcriptomics, proteostasis, unfolded protein response (UPR)

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

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PRIDE project URI

• PRIDE
  1. PXD008529
     1. Label: PRIDE project
     2. Name: Chemical stresses fail to mimic the unfolded protein response resulting from luminal load with unfolded polypeptides