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

doi:10.1126/science.1253168

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 journal › Article › peer-review

125 Scopus citations

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.

Original language	English (US)
Pages (from-to)	360-363
Number of pages	4
Journal	Science
Volume	346
Issue number	6207
DOIs	https://doi.org/10.1126/science.1253168
State	Published - Oct 17 2014

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title = "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.",

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AU - Baird, Nathan A.

AU - Douglas, Peter M.

AU - Simic, Milos S.

AU - Grant, Ana R.

AU - Moresco, James J.

AU - Wolff, Suzanne C.

AU - Yates, John R.

AU - Manning, Gerard

AU - Dillin, Andrew

PY - 2014/10/17

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

Abstract

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