Chemical Biology Framework to Illuminate Proteostasis

© 2020 Annual Reviews Inc.. All rights reserved. Protein folding in the cell is mediated by an extensive network of >1,000 chaperones, quality control factors, and trafficking mechanisms collectively termed the proteostasis network. While the components and organization of this network are genera...

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Main Authors: Sebastian, Rebecca M, Shoulders, Matthew D
Format: Article
Language:English
Published: Annual Reviews 2021
Online Access:https://hdl.handle.net/1721.1/136294
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author Sebastian, Rebecca M
Shoulders, Matthew D
author_facet Sebastian, Rebecca M
Shoulders, Matthew D
author_sort Sebastian, Rebecca M
collection MIT
description © 2020 Annual Reviews Inc.. All rights reserved. Protein folding in the cell is mediated by an extensive network of >1,000 chaperones, quality control factors, and trafficking mechanisms collectively termed the proteostasis network. While the components and organization of this network are generally well established, our understanding of how protein-folding problems are identified, how the network components integrate to successfully address challenges, and what types of biophysical issues each proteostasis network component is capable of addressing remains immature. We describe a chemical biology-informed framework for studying cellular proteostasis that relies on selection of interesting protein-folding problems and precise researcher control of proteostasis network composition and activities. By combining these methods with multifaceted strategies to monitor protein folding, degradation, trafficking, and aggregation in cells, researchers continue to rapidly generate new insights into cellular proteostasis.
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spelling mit-1721.1/1362942021-10-28T05:00:04Z Chemical Biology Framework to Illuminate Proteostasis Sebastian, Rebecca M Shoulders, Matthew D © 2020 Annual Reviews Inc.. All rights reserved. Protein folding in the cell is mediated by an extensive network of >1,000 chaperones, quality control factors, and trafficking mechanisms collectively termed the proteostasis network. While the components and organization of this network are generally well established, our understanding of how protein-folding problems are identified, how the network components integrate to successfully address challenges, and what types of biophysical issues each proteostasis network component is capable of addressing remains immature. We describe a chemical biology-informed framework for studying cellular proteostasis that relies on selection of interesting protein-folding problems and precise researcher control of proteostasis network composition and activities. By combining these methods with multifaceted strategies to monitor protein folding, degradation, trafficking, and aggregation in cells, researchers continue to rapidly generate new insights into cellular proteostasis. 2021-10-27T20:34:45Z 2021-10-27T20:34:45Z 2020 2021-07-07T16:25:47Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/136294 en 10.1146/ANNUREV-BIOCHEM-013118-111552 Annual Review of Biochemistry Creative Commons Attribution-Noncommercial-Share Alike http://creativecommons.org/licenses/by-nc-sa/4.0/ application/pdf Annual Reviews PMC
spellingShingle Sebastian, Rebecca M
Shoulders, Matthew D
Chemical Biology Framework to Illuminate Proteostasis
title Chemical Biology Framework to Illuminate Proteostasis
title_full Chemical Biology Framework to Illuminate Proteostasis
title_fullStr Chemical Biology Framework to Illuminate Proteostasis
title_full_unstemmed Chemical Biology Framework to Illuminate Proteostasis
title_short Chemical Biology Framework to Illuminate Proteostasis
title_sort chemical biology framework to illuminate proteostasis
url https://hdl.handle.net/1721.1/136294
work_keys_str_mv AT sebastianrebeccam chemicalbiologyframeworktoilluminateproteostasis
AT shouldersmatthewd chemicalbiologyframeworktoilluminateproteostasis