Recent advances in bioanalytical methods to measure proteome stability in cells

Proteome stability constitutes an essential aspect of protein homeostasis (proteostasis). Proteostasis networks maintain proteins and their interactors in a defined conformation for their activity, localisation, and function. However, endogenous or exogenous stressors can perturb proteostasis integr...

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Bibliographic Details
Published in:Analyst (London) 2021-04, Vol.146 (7), p.297-219
Main Authors: Zhang, Shouxiang, Greening, David W, Hong, Yuning
Format: Article
Language:English
Subjects:
Biological activity
Folding
Homeostasis
Humans
Neurodegenerative Diseases
Protein Folding
Protein Stability
Proteins
Proteome - metabolism
Proteostasis
Proteostasis Deficiencies
Stability
Toxic diseases
Toxicity
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Summary:Proteome stability constitutes an essential aspect of protein homeostasis (proteostasis). Proteostasis networks maintain proteins and their interactors in a defined conformation for their activity, localisation, and function. However, endogenous or exogenous stressors can perturb proteostasis integrity and deplete folding capacity, generating destabilized folding intermediates and deleterious aggregated species. Over the years, protein unfolding, misfolding and aggregation have been reported to be associated with aging and many diseases such as neurodegenerative diseases, diabetes, cardiac disease and toxicity, and cancers. Therefore, monitoring proteome stability is central to understanding underlying biological processes and mechanisms of disease progression. Herein, we review the recent bioanalytical methods to measure protein stability in cells on a proteome-wide scale. This review summarizes recent bioanalytical methods for measuring and profiling protein stability in cells on a proteome-wide scale, which can provide insights for proteostasis and associated diseases.
ISSN:0003-2654
1364-5528
DOI:10.1039/d0an01547d