PXD023488 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Non-lethal stress-induced discrete proteolysis is caspase-3/7 dependent |
| Description | Cells are in constant adaptation to environmental changes to insure their proper functioning. When exposed to stresses, cells activate specific pathways to elicit adaptive modifications. Those changes can be mediated by selective modulation of gene and protein expression as well as by post-translational modifications, such as phosphorylation and proteolytic processing. Protein cleavage, as a controlled and limited post-translational modification, is involved in diverse physiological processes such as the maintenance of protein homeostasis, activation of repair pathways, apoptosis and the regulation of proliferation. Here we assessed by quantitative proteomics the proteolytic landscape in two cell lines subjected to low cisplatin concentrations used as a mild non-lethal stress paradigm. This landscape was compared to the one obtained in the same cells stimulated with cisplatin concentrations inducing apoptosis. These analyses were performed in wild-type cells and in cells lacking the two main executioner caspases: caspase-3 and caspase-7. Ninety proteins were found to be cleaved at one or a few sites (discrete cleavage) in low stress conditions compared to four hundred and forty in apoptotic cells. Many of the cleaved proteins in stressed cells were also found to be cleaved in apoptotic conditions. As expected in apoptotic cells, ~80% of the cleavage events were dependent on caspase 3/caspase 7. Strikingly, upon exposure to non-lethal stresses, no discrete cleavage was detected in cells lacking caspase-3 and caspase-7. This indicates that the proteolytic landscape in stressed viable cells fully depends on the activity of executioner caspases. These results suggest that the so-called executioner caspases fulfill important stress adaptive responses distinct from their role in apoptosis. |
| HostingRepository | PRIDE |
| AnnounceDate | 2021-07-07 |
| AnnouncementXML | Submission_2021-07-07_04:39:54.300.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Manfredo Quadroni |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
| ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
| Instrument | Q Exactive |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2021-01-08 06:03:08 | ID requested | |
| ⏵ 1 | 2021-07-07 04:39:54 | announced | |
| 2 | 2021-07-07 21:28:42 | announced | 2021-07-08: Updated project metadata. |
Publication List
Keyword List
| submitter keyword: proteomics |
| QExactive |
| human |
| proteolysis |
| apoptosis |
Contact List
| Christian Widmann |
| contact affiliation | Department of Biomedical Sciences University of Lausanne Bugnon 7 1005 Lausanne Switzerland |
| contact email | Christian.Widmann@unil.ch |
| lab head | |
| Manfredo Quadroni |
| contact affiliation | University of Lausanne |
| contact email | manfredo.quadroni@unil.ch |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
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| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD023488
- Label: PRIDE project
- Name: Non-lethal stress-induced discrete proteolysis is caspase-3/7 dependent