PXD003264 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Identification of potential mitochondrial CLPXP protease interactors and substrates |
Description | Maintenance of mitochondria is achieved by several mechanisms, including the regulation of mitochondrial proteostasis. The matrix protease CLPXP, involved in protein quality control, has been implicated in ageing and disease. However, particularly due to the lack of knowledge of CLPXP’s substrate spectrum, only little is known about the pathways and mechanisms controlled by this protease. Here we report the first comprehensive identification of potential mitochondrial CLPXP in vivo interaction partners and substrates using a combination of tandem affinity purification and differential proteomics. This analysis reveals that CLPXP in the fungal ageing model Podospora anserina is mainly associated with metabolic pathways in mitochondria, e.g. components of the pyruvate dehydrogenase complex and the tricarboxylic acid cycle as well as subunits of electron transport chain complex I. These data suggest a possible function of mitochondrial CLPXP in the control and/or maintenance of energy metabolism. Since bioenergetic alterations are a common feature of neurodegenerative diseases, cancer, and ageing, our data comprise an important resource for specific studies addressing the role of CLPXP in these adverse processes. |
HostingRepository | PRIDE |
AnnounceDate | 2016-07-27 |
AnnouncementXML | Submission_2016-07-27_00:03:47.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Julian Langer |
SpeciesList | scientific name: Podospora; NCBI TaxID: 5144; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive; LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-12-01 05:20:35 | ID requested | |
⏵ 1 | 2016-07-27 00:03:50 | announced | |
Publication List
Fischer F, Langer JD, Osiewacz HD, Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism. Sci Rep, 5():18375(2015) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: CLPXP protease, Aging, Mitochondria |
Contact List
Julian David Langer |
contact affiliation | MPIs for Biophysics and Brain Research |
contact email | julian.langer@biophys.mpg.de |
lab head | |
Julian Langer |
contact affiliation | MPIs for Biophysics and Brain Research |
contact email | julian.langer@biophys.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2016/07/PXD003264 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD003264
- Label: PRIDE project
- Name: Identification of potential mitochondrial CLPXP protease interactors and substrates