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Chaperones and Proteostasis: Role in Parkinson’s Disease

Proper folding to attain a defined three-dimensional structure is a prerequisite for the functionality of a protein. Improper folding that eventually leads to formation of protein aggregates is a hallmark of several neurodegenerative disorders. Loss of protein homeostasis triggered by cellular stres...

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Autores principales: Joshi, Neha, Raveendran, Atchaya, Nagotu, Shirisha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349525/
https://www.ncbi.nlm.nih.gov/pubmed/32580484
http://dx.doi.org/10.3390/diseases8020024
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author Joshi, Neha
Raveendran, Atchaya
Nagotu, Shirisha
author_facet Joshi, Neha
Raveendran, Atchaya
Nagotu, Shirisha
author_sort Joshi, Neha
collection PubMed
description Proper folding to attain a defined three-dimensional structure is a prerequisite for the functionality of a protein. Improper folding that eventually leads to formation of protein aggregates is a hallmark of several neurodegenerative disorders. Loss of protein homeostasis triggered by cellular stress conditions is a major contributing factor for the formation of these toxic aggregates. A conserved class of proteins called chaperones and co-chaperones is implicated in maintaining the cellular protein homeostasis. Expanding the body of evidence highlights the role of chaperones as central mediators in the formation, de-aggregation and degradation of the aggregates. Altered expression and function of chaperones is associated with many neurodegenerative diseases including Parkinson’s disease. Several studies indicate that chaperones are at the center of the cause and effect cycle of this disease. An overview of the various chaperones that are associated with homeostasis of Parkinson’s disease-related proteins and their role in pathogenicity will be discussed in this review.
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spelling pubmed-73495252020-07-14 Chaperones and Proteostasis: Role in Parkinson’s Disease Joshi, Neha Raveendran, Atchaya Nagotu, Shirisha Diseases Review Proper folding to attain a defined three-dimensional structure is a prerequisite for the functionality of a protein. Improper folding that eventually leads to formation of protein aggregates is a hallmark of several neurodegenerative disorders. Loss of protein homeostasis triggered by cellular stress conditions is a major contributing factor for the formation of these toxic aggregates. A conserved class of proteins called chaperones and co-chaperones is implicated in maintaining the cellular protein homeostasis. Expanding the body of evidence highlights the role of chaperones as central mediators in the formation, de-aggregation and degradation of the aggregates. Altered expression and function of chaperones is associated with many neurodegenerative diseases including Parkinson’s disease. Several studies indicate that chaperones are at the center of the cause and effect cycle of this disease. An overview of the various chaperones that are associated with homeostasis of Parkinson’s disease-related proteins and their role in pathogenicity will be discussed in this review. MDPI 2020-06-22 /pmc/articles/PMC7349525/ /pubmed/32580484 http://dx.doi.org/10.3390/diseases8020024 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Joshi, Neha
Raveendran, Atchaya
Nagotu, Shirisha
Chaperones and Proteostasis: Role in Parkinson’s Disease
title Chaperones and Proteostasis: Role in Parkinson’s Disease
title_full Chaperones and Proteostasis: Role in Parkinson’s Disease
title_fullStr Chaperones and Proteostasis: Role in Parkinson’s Disease
title_full_unstemmed Chaperones and Proteostasis: Role in Parkinson’s Disease
title_short Chaperones and Proteostasis: Role in Parkinson’s Disease
title_sort chaperones and proteostasis: role in parkinson’s disease
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349525/
https://www.ncbi.nlm.nih.gov/pubmed/32580484
http://dx.doi.org/10.3390/diseases8020024
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