PXD017482

PXD017482 is an original dataset announced via ProteomeXchange.

Title	A High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs)
Description	The voltage-dependent anion-selective channels (VDACs), also known as eukaryotic porins, are pore-forming proteins which allow the passage of ions and small molecules across the outer mitochondrial membrane (OMM). They are involved in complex interactions regulating organelle and cellular metabolism. We have recently reported about the post-translational modifications (PTMs) of the three VDAC isoforms purified from rat liver mitochondria (rVDACs), showing for the first time the over-oxidation of the cysteine residues as an exclusive feature of VDACs. Noteworthy, this peculiar PTM is not detectable in other integral membrane mitochondrial proteins, as defined by their elution at low salt concentration by a hydroxyapatite column. In this study, the association of tryptic and chymotryptic proteolysis with UHPLC/High Resolution nESI-MS/MS, allowed us to extend the investigation to the human VDACs. Over-oxidation of the cysteine residues, essentially irreversible in cell conditions, was as certained also in VDAC isoforms from human cells. In human VDAC2 and 3 isoforms the permanently reduced state of a cluster of close cysteines indicates the possibility that disulfide bridges are formed in the proteins. Importantly, the detailed oxidative PTMs found in human VDACs confirm and sustain our previous findings in rat tissues, claiming for a predictable characterization that has to be conveyed in the functional role of VDAC proteins within the cell.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:00:02.147.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Rosaria Saletti
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2020-02-12 03:16:04	ID requested
1	2020-03-09 00:40:10	announced
⏵ 2	2024-10-22 05:00:05	announced	2024-10-22: Updated project metadata.

Pittal, à MGG, Saletti R, Reina S, Cunsolo V, De Pinto V, Foti S, A High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs). Int J Mol Sci, 21(4):(2020) [pubmed]

10.3390/ijms21041468;

submitter keyword: Cysteine over-oxidation

mitochondria

Orbitrap Fusion Tribrid

hydroxyapatite

mitochondrial intermembrane space

outer mitochondrial membrane

post-translational modification

Salvatore Foti
contact affiliation	Organic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania
contact email	sfoti@unict.it
lab head
Rosaria Saletti
contact affiliation	University of Catania
contact email	rsaletti@unict.it
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/2020/03/PXD017482

PRIDE project URI

• PRIDE
  1. PXD017482
     1. Label: PRIDE project
     2. Name: A High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs)