PXD030782

PXD030782 is an original dataset announced via ProteomeXchange.

Title	Peroxisome-derived hydrogen peroxide can modulate the sulfenylation profiles of key redox signaling proteins in Flp-In T-REx 293 cells
Description	Ever since the first characterization of peroxisomes, a central theme has been their involvement in cellular hydrogen peroxide (H2O2) metabolism. While the reputation of H2O2 drastically changed from an exclusively toxic molecule to a signaling messenger, the regulatory role of peroxisomes in these signaling events is still largely underappreciated. This is mainly because the number of known protein targets of peroxisome-derived H2O2 is rather limited and testing of specific targets is predominantly based on knowledge previously gathered in related fields of research. To gain a broader and more systematic insight into the role of peroxisomes in redox signaling, new approaches are urgently needed. In this study, we have combined a previously developed Flp-In T-REx 293 cell system in which peroxisomal H2O2 production can be modulated with a yeast AP-1-like-based sulfenome mining strategy to inventory protein thiol targets of peroxisome-derived H2O2 in different subcellular compartments. Using this approach, we were able to identify specific and common targets of peroxisome-derived and exogenous H2O2 in peroxisomes, the cytosol, and mitochondria. We also observed that the sulfenylation kinetics profiles of key targets (e.g., PRDX1, ANXA2, and TUBA1C) belonging to different protein families (e.g., antioxidants, annexins, and tubulins) can vary considerably. In addition, we obtained compelling but indirect evidence that peroxisome-derived H2O2 may oxidize at least some of its targets (e.g., transcription factors) through a redox relay mechanism. In conclusion, given that sulfenic acids function as key intermediates in H2O2 signaling, the findings presented in this study provide initial but critical insight into how peroxisomes may be integrated into the cellular H2O2 signaling network.
HostingRepository	PRIDE
AnnounceDate	2022-05-10
AnnouncementXML	Submission_2022-05-10_07:25:29.927.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD030782
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Celien Lismont
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; N-methylmaleimide modified L-cysteine; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-01-06 01:50:36	ID requested
⏵ 1	2022-05-10 07:25:30	announced

Dataset with its publication pending

submitter keyword: Peroxisome

hydrogen peroxide

cysteine thiol group

YAP1C-based sulfenome mining

peroxiredoxin

mitochondrion

Marc Fransen
contact affiliation	Department of cellular and molecular medicine, Laboratory of peroxisome biology and intracellular communication, KU Leuven, Belgium
contact email	marc.fransen@kuleuven.be
lab head
Celien Lismont
contact affiliation	KU Leuven
contact email	celien.lismont@kuleuven.be
dataset submitter

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/2022/05/PXD030782

PRIDE project URI

• PRIDE
  1. PXD030782
     1. Label: PRIDE project
     2. Name: Peroxisome-derived hydrogen peroxide can modulate the sulfenylation profiles of key redox signaling proteins in Flp-In T-REx 293 cells