PXD036728 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Specific post-translational modifications of VDAC3 in ALS-SOD1 model cells identified by High-Resolution Mass Spectrometry |
Description | Damage induced by oxidative stress is a key driver of the selective motor neuron death in amyotrophic lateral sclerosis (ALS). Mitochondria are among the main producers of ROS, but they also suffer particularly from their harmful effects. Voltage-dependent anion-selective channels (VDACs) are the most represented proteins of the outer mitochondrial membrane where they form pores controlling the permeation of metabolites responsible for mitochondrial functions. For these reasons, VDACs contribute to mitochondrial quality control and the entire energy metabolism of the cell. In this work we assessed whether oxidative stress in ALS induces post-translational modifications (PTMs) in VDAC3, a member of the VDAC family of outer mitochondrial membrane channel proteins, known for its role in redox signaling. At this end, protein samples enriched in VDACs were prepared from mitochondria of an ALS model cell line, NSC34 expressing human SOD1G93A, and analyzed by nUHPLC/High-Resolution nESI-MS/MS. Specific over-oxidation, deamidation, succination events were found in VDAC3 from ALS-related NSC34-SOD1G93A but not in non-ALS cell lines. We also report evidence that some PTMs may affect VDAC3 functionality. In particular, deamidation of Asn215 alone results in channel instability. Overall, our results suggest modifications of VDAC3 that can impact its protective role against ROS, which is particularly important in the ALS context. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_08:43:33.088.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Rosaria Saletti |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
ModificationList | acetylated residue; monohydroxylated residue; deaminated residue; deamidated residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-09-14 03:21:08 | ID requested | |
1 | 2023-03-11 10:46:30 | announced | |
⏵ 2 | 2023-11-14 08:43:41 | announced | 2023-11-14: Updated project metadata. |
Publication List
Pittal, à MGG, Reina S, Nibali SC, Cucina A, Cubisino SAM, Cunsolo V, Amodeo GF, Foti S, De Pinto V, Saletti R, Messina A, Specific Post-Translational Modifications of VDAC3 in ALS-SOD1 Model Cells Identified by High-Resolution Mass Spectrometry. Int J Mol Sci, 23(24):(2022) [pubmed] |
Keyword List
submitter keyword: Deamidation |
Amyotrophic Lateral Sclerosis |
Voltage Dependent Anion Channel |
post-translational modifications |
mitochondria |
ROS |
Mass Spectrometry analysis |
Orbitrap fusion tribrid |
neurodegeneration |
SOD1. |
Contact List
Rosaria Saletti |
contact affiliation | Organic Mass Spectrometry Laboratory, Department of Chemical Sciences, University of Catania, Via S. Sofia 64, 95123 Catania, Italy |
contact email | rsaletti@unict.it |
lab head | |
Rosaria Saletti |
contact affiliation | University of Catania |
contact email | rsaletti@unict.it |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD036728
- Label: PRIDE project
- Name: Specific post-translational modifications of VDAC3 in ALS-SOD1 model cells identified by High-Resolution Mass Spectrometry