Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 84
Volume 84, Issue -, Pages 435-464Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060614-033955
Keywords
chaperones; protein folding; stress response; neurodegenerative disease; protein misfolding; aggregation
Categories
Funding
- NIA NIH HHS [R37 AG026647, R01 AG026647] Funding Source: Medline
- NIGMS NIH HHS [P50 GM081892, R37 GM038109, R01 GM038109] Funding Source: Medline
- NIMH NIH HHS [P50 MH094267] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM038109, R37GM038109, P50GM081892] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF MENTAL HEALTH [P50MH094267] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON AGING [R37AG026647, R01AG026647] Funding Source: NIH RePORTER
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Loss of protein homeostasis (proteostasis) is a common feature of aging and disease that is characterized by the appearance of nonnative protein aggregates in various tissues. Protein aggregation is routinely suppressed by the proteostasis network (PN), a collection of macromolecular machines that operate in diverse ways to maintain proteome integrity across subcellular compartments and between tissues to ensure a healthy life span. Here, we review the composition, function, and organizational properties of the PN in the context of individual cells and entire organisms and discuss the mechanisms by which disruption of the PN, and related stress response pathways, contributes to the initiation and progression of disease. We explore emerging evidence that disease susceptibility arises from early changes in the composition and activity of the PN and propose that a more complete understanding of the temporal and spatial properties of the PN will enhance our ability to develop effective treatments for protein conformational diseases.
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