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HSF-1-mediated cytoskeletal integrity determines thermotolerance and life span.


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.

SUBMITTER: Baird NA 

PROVIDER: S-EPMC4403873 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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HSF-1-mediated cytoskeletal integrity determines thermotolerance and life span.

Baird Nathan A NA   Douglas Peter M PM   Simic Milos S MS   Grant Ana R AR   Moresco James J JJ   Wolff Suzanne C SC   Yates John R JR   Manning Gerard G   Dillin Andrew A  

Science (New York, N.Y.) 20141001 6207


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  ...[more]

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