Wright, Gareth SA 
ORCID: 0000-0002-3756-9634
(2020)
Molecular and pharmacological chaperones for SOD1.
BIOCHEMICAL SOCIETY TRANSACTIONS, 48 (4).
pp. 1795-1806.
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Abstract
The efficacy of superoxide dismutase-1 (SOD1) folding impacts neuronal loss in motor system neurodegenerative diseases. Mutations can prevent SOD1 post-translational processing leading to misfolding and cytoplasmic aggregation in familial amyotrophic lateral sclerosis (ALS). Evidence of immature, wild-type SOD1 misfolding has also been observed in sporadic ALS, non-SOD1 familial ALS and Parkinson's disease. The copper chaperone for SOD1 (hCCS) is a dedicated and specific chaperone that assists SOD1 folding and maturation to produce the active enzyme. Misfolded or misfolding prone SOD1 also interacts with heat shock proteins and macrophage migration inhibitory factor to aid folding, refolding or degradation. Recognition of specific SOD1 structures by the molecular chaperone network and timely dissociation of SOD1-chaperone complexes are, therefore, important steps in SOD1 processing. Harnessing these interactions for therapeutic benefit is actively pursued as is the modulation of SOD1 behaviour with pharmacological and peptide chaperones. This review highlights the structural and mechanistic aspects of a selection of SOD1-chaperone interactions together with their impact on disease models.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Animals, Humans, Copper, Heat-Shock Proteins, Molecular Chaperones, Macrophage Migration-Inhibitory Factors, Protein Folding, Mutation, Superoxide Dismutase-1 |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 22 Apr 2021 06:58 |
| Last Modified: | 18 Jan 2023 22:51 |
| DOI: | 10.1042/BST20200318 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3120095 |
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