PXD024687-1

PXD024687 is an original dataset announced via ProteomeXchange.

Title	Oxidation of peroxiredoxin-4 induces oligomerization and promotes interaction with endoplasmic reticulum proteins
Description	The family of peroxiredoxins catalyzes the reduction of hydrogen peroxide (H2O2). Peroxiredoxin 4 (PRDX4) is the only peroxiredoxin located within the endoplasmic reticulum (ER) and is the highest expressed ER H2O2 scavenger. PRDX4 has emerged as an important player in numerous diseases and its over-oxidation is a potential indicator of ER redox stress. The interactome of PRDX4 as well as the dynamics of its oligomerization have largely been unstudied. Therefore, the goal of this study was to determine the effect of oxidation on PRDX4 oligomerization and interaction with binding partners. We report that the oxidation of PRDX4 in lung epithelial cells treated with tertbutyl hydroperoxide (TBuOOH) caused a shift of PRDX4 from monomer/dimer to high molecular weight(HMW) species which are composed of PRDX4 containing sulfonic acid residues (PRDX4-SO3) as well as a complement of ER-associated proteins. Treatment of recombinant PRDX4 with TBuOOH also led to HMW complexes, showing that interactions with client proteins are not required for PRDX4 HMW complex formation.
HostingRepository	PRIDE
AnnounceDate	2022-02-17
AnnouncementXML	Submission_2022-02-16_16:58:24.068.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD024687
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Evan Elko
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	N-ethylmaleimide derivatized cysteine; L-cysteine sulfinic acid; monohydroxylated residue; L-cysteic acid (L-cysteine sulfonic acid); iodoacetamide derivatized residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2021-03-11 23:05:30	ID requested
⏵ 1	2022-02-16 16:58:24	announced

Elko EA, Manuel AM, White S, Zito E, van der Vliet A, Anathy V, Janssen-Heininger YMW, Oxidation of peroxiredoxin-4 induces oligomerization and promotes interaction with proteins governing protein folding and endoplasmic reticulum stress. J Biol Chem, 296():100665(2021) [pubmed]

submitter keyword: Prdx4, Tert-butyl hydroperoxide

Yvonne Janssen-Heininger
contact affiliation	University of Vermont, Department of Pathology and Laboratory Medicine
contact email	yvonne.janssen@med.uvm.edu
lab head
Evan Elko
contact affiliation	University of Vermont
contact email	eelko@uvm.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD024687
     1. Label: PRIDE project
     2. Name: Oxidation of peroxiredoxin-4 induces oligomerization and promotes interaction with endoplasmic reticulum proteins