Heat shock factor-1 alleviates ER-stress in Caenorhabditis elegans.

Saqib Ahmed, Dániel Kovács, Márton Kovács, Mónika Kosztelnik, Bernadette Hotzi, Tímea Sigmond, Éva Saskői, Viktor Vázsony Vincze, Viktor Erdélyi, Veronika Deák, Ibolya Stiller, Tibor Vellai, János Barna

Department of Genetics, Institute of Biology, Eötvös Loránd University, Budapest, Hungary. · pubmed

Paper

Abstract

Cells can be exposed to many different stimuli that induce a variety of stresses, such as oxidative stress and proteotoxic stress of the cytoplasm, endoplasmic reticulum or mitochondria. These types of stresses trigger conserved molecular pathways (e.g., heat shock response, unfolded protein response, and autophagy) that can restore cellular homeostasis. Dysfunction (deficiency or hyperactivity) of these pathways is associated with aging and pathologies such as neurodegenerative diseases, diabetes and cancer. The basic molecular machinery of these stress response pathways has been elucidated, but how these pathways interact remains a vibrant area of research. Here, we show that the heat shock transcription factor-1 (HSF-1), the master regulator of the heat shock response, is required for efficient activation of the endoplasmic reticulum unfolded protein response (UPR

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Research summary

The paper claims that heat shock factor-1 (HSF-1) is essential for the effective activation of the endoplasmic reticulum unfolded protein response (UPR). This research is relevant as it explores the molecular pathways involved in cellular stress responses, which are linked to aging and age-related diseases, potentially addressing root causes of aging.

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