Targeting the Mitochondrial Protein VDAC1 as a Potential Therapeutic Strategy in ALS.
ALS
VDAC1
apoptosis
misfolded proteins
mitochondria
mutant SOD1
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
01 Sep 2022
01 Sep 2022
Historique:
received:
26
05
2022
revised:
25
08
2022
accepted:
26
08
2022
entrez:
9
9
2022
pubmed:
10
9
2022
medline:
14
9
2022
Statut:
epublish
Résumé
Impaired mitochondrial function has been proposed as a causative factor in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), caused by motor neuron degeneration. Mutations in superoxide dismutase (SOD1) cause ALS and SOD1 mutants were shown to interact with the voltage-dependent anion channel 1 (VDAC1), affecting its normal function. VDAC1 is a multi-functional channel located at the outer mitochondrial membrane that serves as a mitochondrial gatekeeper controlling metabolic and energetic crosstalk between mitochondria and the rest of the cell and it is a key player in mitochondria-mediated apoptosis. Previously, we showed that VDAC1 interacts with SOD1 and that the VDAC1-N-terminal-derived peptide prevented mutant SOD1 cytotoxic effects. In this study, using a peptide array, we identified the SOD1 sequence that interacts with VDAC1. Synthetic peptides generated from the identified VDAC1-binding sequences in SOD1 directly interacted with purified VDAC1. We also show that VDAC1 oligomerization increased in spinal cord mitochondria isolated from mutant SOD1
Identifiants
pubmed: 36077343
pii: ijms23179946
doi: 10.3390/ijms23179946
pmc: PMC9456491
pii:
doi:
Substances chimiques
Mitochondrial Proteins
0
Vdac1 protein, rat
0
Superoxide Dismutase
EC 1.15.1.1
Superoxide Dismutase-1
EC 1.15.1.1
Voltage-Dependent Anion Channel 1
EC 1.6.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Israel Science Foundation
ID : 284/19
Organisme : Israel Science Foundation
ID : 974/19
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