A VDAC1-Derived N-Terminal Peptide Inhibits Mutant SOD1-VDAC1 Interactions and Toxicity in the SOD1 Model of ALS.
ALS
N-terminal peptide
VDAC1
misfolded SOD1
mutant SOD1
Journal
Frontiers in cellular neuroscience
ISSN: 1662-5102
Titre abrégé: Front Cell Neurosci
Pays: Switzerland
ID NLM: 101477935
Informations de publication
Date de publication:
2019
2019
Historique:
received:
20
01
2019
accepted:
15
07
2019
entrez:
3
9
2019
pubmed:
3
9
2019
medline:
3
9
2019
Statut:
epublish
Résumé
Mutations in superoxide dismutase (SOD1) are the second most common cause of familial amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease caused by the death of motor neurons in the brain and spinal cord. SOD1 neurotoxicity has been attributed to aberrant accumulation of misfolded SOD1, which in its soluble form binds to intracellular organelles, such as mitochondria and ER, disrupting their functions. Here, we demonstrate that mutant SOD1 binds specifically to the N-terminal domain of the voltage-dependent anion channel (VDAC1), an outer mitochondrial membrane protein controlling cell energy, metabolic and survival pathways. Mutant SOD1
Identifiants
pubmed: 31474832
doi: 10.3389/fncel.2019.00346
pmc: PMC6702328
doi:
Types de publication
Journal Article
Langues
eng
Pagination
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