Mechanisms of protein-folding diseases at a glance
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Lindquist_Mechanisms of protein.pdf
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728.25 KB
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Author(s)
Valastyan, Julie Suzanne
Lindquist, Susan
Date Issued
January 2014
Journal
Disease Models & Mechanisms
Publisher
Company of Biologists
Citation
Valastyan, J. S., and S. Lindquist. “Mechanisms of protein-folding diseases at a glance.” Disease Models & Mechanisms 7, no. 1 (January 6, 2014): 9-14.
Version
Final published version
Abstract
For a protein to function appropriately, it must first achieve its proper conformation and location within the crowded environment inside the cell. Multiple chaperone systems are required to fold proteins correctly. In addition, degradation pathways participate by destroying improperly folded proteins. The intricacy of this multisystem process provides many opportunities for error. Furthermore, mutations cause misfolded, nonfunctional forms of proteins to accumulate. As a result, many pathological conditions are fundamentally rooted in the protein-folding problem that all cells must solve to maintain their function and integrity. Here, to illustrate the breadth of this phenomenon, we describe five examples of protein-misfolding events that can lead to disease: improper degradation, mislocalization, dominant-negative mutations, structural alterations that establish novel toxic functions, and amyloid accumulation. In each case, we will highlight current therapeutic options for battling such diseases.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
Terms of Use
Creative Commons Attribution
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1242/dmm.013474
