Chemical Biology Framework to Illuminate Proteostasis
Name
nihms-1583690.pdf
Description
Accepted version
Size
1.69 MB
Format
Unknown
Checksum (MD5)
bd2d8fc36e00aea3cdf3f894cd8ea460
Author(s)
Sebastian, Rebecca M.
Shoulders, Matthew D.
Date Issued
June 2020
Journal
Annual Review of Biochemistry
Publisher
Annual Reviews
Version
Author's final manuscript
Abstract
© 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.
Subjects
Biochemistry
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1146/annurev-biochem-013118-111552
