PXD003264

PXD003264 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2015-12-01 05:20:35	ID requested
⏵ 1	2016-07-27 00:03:50	announced

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]

curator keyword: Biological

submitter keyword: CLPXP protease, Aging, Mitochondria

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

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PRIDE project URI

• PRIDE
  1. PXD003264
     1. Label: PRIDE project
     2. Name: Identification of potential mitochondrial CLPXP protease interactors and substrates