PXD024114

PXD024114 is an original dataset announced via ProteomeXchange.

Title	The Human 2-Cys Peroxiredoxins Form Widespread, Cysteine-Dependent- And Isoform-Specific Protein-Protein Interactions.
Description	Redox signaling is controlled by the reversible oxidation of cysteine thiols, a post-translational modification triggered by H2O2 acting as a second messenger. However, H2O2 reacts poorly with most cysteine thiols and it is not clear how it discriminates between cysteines to trigger appropriate signaling cascades in the presence of dedicated H2O2 scavengers like peroxiredoxins. It was suggested that peroxiredoxins act as peroxidases to facilitate H2O2-dependent oxidation of proteins via disulfide exchange reactions. It is unknown how the peroxiredoxin-based relay model achieves the selective substrate targeting required for adequate cellular signaling. Using a systematic mass-spectrometry-based approach to identify cysteine-dependent interactors of peroxiredoxins, we show that all five human 2-cys peroxiredoxins can form disulfide-dependent heterodimers with a large set of proteins. Each isoform displays a preference for a subset of disulfide-dependent binding partners, and we explore isoform-specific properties that might underlie this precedence. We provide evidence that peroxiredoxin-based redox relays can proceed via two distinct molecular mechanisms. Altogether, our results support the theory that peroxiredoxins could play a role in providing not only reactivity but also selectivity in the transduction of peroxide signals to generate complex cellular signaling responses.
HostingRepository	PRIDE
AnnounceDate	2021-05-04
AnnouncementXML	Submission_2021-05-03_22:09:30.557.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Harmjan Vos
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	N-ethylmaleimide derivatized cysteine; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-02-10 08:04:22	ID requested
⏵ 1	2021-05-03 22:09:31	announced

van Dam L, Pag, è, s-Gallego M, Polderman PE, van Es RM, Burgering BMT, Vos HR, Dansen TB, The Human 2-Cys Peroxiredoxins form Widespread, Cysteine-Dependent- and Isoform-Specific Protein-Protein Interactions. Antioxidants (Basel), 10(4):(2021) [pubmed]

submitter keyword: peroxiredoxin

redox signaling

redox relay, hydrogen peroxide, protein thiol oxidation, cysteine sulfenic acid, thiol disulfide exchange

Tobias B. Dansen
contact affiliation	Center for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
contact email	T.B.Dansen@umcutrecht.nl
lab head
Harmjan Vos
contact affiliation	University Medical Center Utrecht Dept. Molecular Cancer Research
contact email	h.r.vos-3@umcutrecht.nl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD024114
     1. Label: PRIDE project
     2. Name: The Human 2-Cys Peroxiredoxins Form Widespread, Cysteine-Dependent- And Isoform-Specific Protein-Protein Interactions.