PXD064110

PXD064110 is an original dataset announced via ProteomeXchange.

Title	Structural characterization of intra- and intermolecular disulfide bonds in Voltage-Dependent Anion Channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry
Description	Voltage-Dependent Anion Channels, the most abundant proteins of the mitochondrial outer membrane, are responsible for exchange of ions and metabolites between cytosol and mitochondria. They participate in the control of glycolytic metabolism through interaction with numerous enzymes and play a key role in regulation of mitochondria-mediated apoptosis, cancer and neurodegenerative diseases. The structural characterization of VDACs presents difficulties because there is no established protocol for the isolation of a single VDAC isoform and/or separation from other membrane proteins, so they can only be studied as component of a mixture. Recently, we have showed that High-Resolution Mass Spectrometry coupled with UHPLC, represents a powerful tool for their structural characterization. Using this technique we discovered that cysteines in rat and human VDACs show a preferred oxidation state, ranging from reduced to trioxidized form, that is remarkably conserved between rat and human VDACs. More recently, characterization of intramolecular disulfide bonds in rVDAC2 was obtained. The successful characterization of disulfide bonds in rVDAC2, prompted us to use the same procedure for the investigation of intramolecular disulfide bonds in rVDAC3 and also to attempt a possible characterization of intermolecular disulfide bonds formed by this protein with other VDAC isoforms. As a result, three intramolecular and seven intermolecular disulfide bonds between rVDAC3 with rVDAC1 and rVDAC2 were uniquely characterized. Furthermore, evidence was obtained for the existence of two additional intramolecular disulfide bonds between Cys2/Cys8 with Cys36 and Cys122, although these identification were not supported by MS/MS spectra.
HostingRepository	PRIDE
AnnounceDate	2025-09-08
AnnouncementXML	Submission_2025-09-07_16:19:05.578.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rosaria Saletti
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2025-05-20 08:02:12	ID requested
⏵ 1	2025-09-07 16:19:06	announced

10.1007/s00216-025-06074-w;

Pittal, à MGG, Cucina A, Conti-Nibali S, Cunsolo V, Di Francesco A, Battiato G, Reina S, Foti S, De Pinto V, Saletti R, Structural characterization of intra- and intermolecular disulfide bonds in voltage-dependent anion channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry. Anal Bioanal Chem, 417(24):5555-5570(2025) [pubmed]

submitter keyword: High-resolution Mass Spectrometry

Intra- and intermolecular Disulfide Bonds

Rattus Voltage-dependent Anion Selective Channel Isoform 3 (rVDAC3)

Cysteine Redox State

Structural Characterization

Rosaria Saletti
contact affiliation	1Department of Chemical Sciences, Organic Mass Spectrometry Laboratory, University of Catania, Viale A. Doria 6, 95125 Catania, Italy
contact email	rsaletti@unict.it
lab head
Rosaria Saletti
contact affiliation	University of Catania
contact email	rsaletti@unict.it
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD064110
     1. Label: PRIDE project
     2. Name: Structural characterization of intra- and intermolecular disulfide bonds in Voltage-Dependent Anion Channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry