期刊
SCIENCE
卷 346, 期 6207, 页码 360-363出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1253168
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资金
- Howard Hughes Medical Institute, National Center for Research Resources [5P41RR011823-17]
- National Institute of General Medical Sciences [8 P41 GM103533-17]
- National Institute on Aging [R01AG027463-04]
- Leona M. & Harry B. Helmsley Charitable Trust
- George E. Hewitt Foundation for Medical Research
- National Institute of Aging [1K99AG042495-0141]
- NIH-Office of Research Infrastructure Programs [P40 OD010440]
The conserved heat shock transcription factor-1 (HSF-1) is essential to cellular stress resistance and life-span determination. The canonical function of HSF-1 is to regulate a network of genes encoding molecular chaperones that protect proteins from damage caused by extrinsic environmental stress or intrinsic age-related deterioration. In Caenorhabditis elegans, we engineered a modified HSF-1 strain that increased stress resistance and longevity without enhanced chaperone induction. This health assurance acted through the regulation of the calcium-binding protein PAT-10. Loss of pat-10 caused a collapse of the actin cytoskeleton, stress resistance, and life span. Furthermore, overexpression of pat-10 increased actin filament stability, thermotolerance, and longevity, indicating that in addition to chaperone regulation, HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging.
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