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S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions

Conway, Myra E.; Harris, Matthew

S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions Thumbnail


Authors

Myra Conway Myra.Conway@uwe.ac.uk
Occasional Associate Lecturer - CHSS - DAS

Matthew Harris



Abstract

© 2015 Conway and Harris. Correct protein folding and inhibition of protein aggregation is facilitated by a cellular "quality control system" that engages a network of protein interactions including molecular chaperones and the ubiquitin proteasome system. Key chaperones involved in these regulatory mechanisms are the protein disulfide isomerases (PDI) and their homologs, predominantly expressed in the endoplasmic reticulum of most tissues. Redox changes that disrupt ER homeostasis can lead to modification of these enzymes or chaperones with the loss of their proposed neuroprotective role resulting in an increase in protein misfolding. Misfolded protein aggregates have been observed in several disease states and are considered to play a pivotal role in the pathogenesis of neurodegenerative conditions such as Alzheimer's disease, Parkinson's disease, and Amyotrophic Lateral sclerosis. This review will focus on the importance of the thioredoxin-like CGHC active site of PDI and how our understanding of this structural motif will play a key role in unraveling the pathogenic mechanisms that underpin these neurodegenerative conditions.

Journal Article Type Short Survey
Acceptance Date Mar 30, 2015
Publication Date Jan 1, 2015
Deposit Date Nov 16, 2015
Publicly Available Date Feb 25, 2016
Journal Frontiers in Chemistry
Electronic ISSN 2296-2646
Publisher Frontiers Media
Peer Reviewed Peer Reviewed
Volume 3
Issue APR
DOI https://doi.org/10.3389/fchem.2015.00027
Keywords PDI, thioredoxin-like -CXXC- motifs, protein folding, S-nitrosylation, neurodegeneration
Public URL https://uwe-repository.worktribe.com/output/835704
Publisher URL http://dx.doi.org/10.3389/fchem.2015.00027
Additional Information Additional Information : This Document is Protected by copyright and was first published by Frontiers. All rights reserved. it is reproduced with permission.
Contract Date Feb 25, 2016

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