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

Nathan A. Baird, Peter M. Douglas, Milos S. Simic, Ana R. Grant, James J. Moresco, Suzanne C. Wolff, John R. Yates, Gerard Manning, Andrew Dillin

Research output: Contribution to journalArticlepeer-review

115 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)360-363
Number of pages4
Issue number6207
StatePublished - Oct 17 2014

ASJC Scopus subject areas

  • General


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