Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum
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nihms-522926.pdf
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4.52 MB
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Adobe PDF
Checksum (MD5)
973a567f4de3d3ebed1b2cb105416b3f
Author(s)
Ploegh, Hidde
Smith, Melanie H.
Weissman, Jonathan S.
Date Issued
November 2011
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Citation
Smith, M. H., H. L. Ploegh, and J. S. Weissman. “Road to Ruin: Targeting Proteins for Degradation in the Endoplasmic Reticulum.” Science 334, no. 6059 (November 25, 2011): 1086–1090.
Version
Author's final manuscript
Abstract
Some nascent proteins that fold within the endoplasmic reticulum (ER) never reach their native state. Misfolded proteins are removed from the folding machinery, dislocated from the ER into the cytosol, and degraded in a series of pathways collectively referred to as ER-associated degradation (ERAD). Distinct ERAD pathways centered on different E3 ubiquitin ligases survey the range of potential substrates. We now know many of the components of the ERAD machinery and pathways used to detect substrates and target them for degradation. Much less is known about the features used to identify terminally misfolded conformations and the broader role of these pathways in regulating protein half-lives.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
https://doi.org/10.1126/science.1209235
