Evidence map›Paper›PMID 40875006›Full record

ArticleAnalytical and bioanalytical chemistry2025

Structural characterization of intra- and intermolecular disulfide bonds in voltage-dependent anion channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry.

Maria Gaetana Giovanna Pittalà, Annamaria Cucina, Stefano Conti-Nibali, Vincenzo Cunsolo, Antonella Di Francesco, Giuseppe Battiato, Simona Reina, Salvatore Foti, Vito De Pinto, Rosaria Saletti

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Article in Analytical and bioanalytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

10 authors.

Maria Gaetana Giovanna PittalàOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy.
Annamaria CucinaOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy.
Stefano Conti-NibaliSection of Biology and Genetics, Department of Biomedical Sciences and Biotechnology, University of Catania, Via S. Sofia, 97, 95123, Catania, Italy.
Vincenzo CunsoloOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy.
Antonella Di FrancescoOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy.
Giuseppe BattiatoSection of Biology and Genetics, Department of Biomedical Sciences and Biotechnology, University of Catania, Via S. Sofia, 97, 95123, Catania, Italy.
Simona ReinaSection of Biology and Genetics, Department of Biomedical Sciences and Biotechnology, University of Catania, Via S. Sofia, 97, 95123, Catania, Italy.
Salvatore FotiOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy.
Vito De PintoSection of Biology and Genetics, Department of Biomedical Sciences and Biotechnology, University of Catania, Via S. Sofia, 97, 95123, Catania, Italy.
Rosaria SalettiOrganic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, 95125, Catania, Italy. rsaletti@unict.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-dependent anion channels, the most abundant proteins of the mitochondrial outer membrane, are responsible for the 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 the regulation of mitochondria-mediated apoptosis, cancer, and neurodegenerative diseases. The enzymatic digestion procedure in solution, originally developed in our laboratory, followed by high-resolution mass spectrometry coupled with UHPLC, has proven to be a powerful tool for the structural characterization of these "difficult" proteins. In this work, we used this procedure for the localization of intramolecular disulfide bonds in rVDAC3 and also for the 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 identifications were not supported by MS/MS spectra. The formation of intermolecular disulfide bonds helps to explain the previously observed VDAC oligomerization and demonstrates that disulfide bridges are directly involved in their homo- or hetero-oligomerization. Data are available via ProteomeXchange with identifier PXD064110.

Indexed as

DisulfidesVoltage-Dependent Anion ChannelsAmino Acid SequenceAnimalsChromatography, High Pressure LiquidMass SpectrometryRatsTandem Mass SpectrometryDisulfidesVoltage-Dependent Anion ChannelsCysteine redox stateHigh-resolution mass spectrometryIntra- and intermolecular disulfide bondsRattus voltage-dependent anion selective channel isoform 3 (rVDAC3)Structural characterization

Identifiers

PMID40875006
PMCPMC12521285

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