HSF-1-mediated cytoskeletal integrity determines thermotolerance and life span.
basic_science · Level V
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- Record sourced from PubMed, PMID 25324391.
- Also identified by DOI 10.1126/science.1253168 and PMC identifier 4403873.
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Abstract
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.
Medical subject headings
- Caenorhabditis elegans
- Caenorhabditis elegans Proteins
- Cytoskeleton
- Heat-Shock Response
- Longevity
- Transcription Factors
- Troponin C