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Updated: Jan 8, 2026

Measurements of Physiological Stress Responses in C. Elegans

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

メカノセンサーを介したHsp70リン酸化による熱ショック応答の様相の調整

Siddhi Omkar¹, Jake T Kline², James H Grissom¹

¹Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC, USA.

Nature communications

|December 13, 2025

Abstract:

Cells must respond rapidly to heat stress by activating multiple signaling pathways that preserve proteostasis. In budding yeast, this includes induction of Hsf1 and Msn2/4-mediated transcription, cell integrity signaling, stress-triggered phase separation of proteins, and inhibition of translation. How these pathways are so rapidly activated and coordinated remains unclear. We show that the mechanosensor Mid2 senses heat-induced membrane stretch and leads to rapid phosphorylation of the cytosolic Hsp70 Ssa1 at a well-conserved threonine (T492). Phosphorylation of T492 leads to epichaperome rearrangement promoting fine-tuning of multiple cellular processes including translational pausing, HSF activity, MAPK signaling and stress granule resolution. Taken together, these results provide a comprehensive, unified theory of the global yeast heat shock response mediated by the Hsp70 chaperone code.

キーワード:

酵母熱ショック応答メカノセンサー Hsp70 リン酸化タンパク質恒常性翻訳の一時停止 HSF活性化

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Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans

Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans

Published on: July 3, 2020

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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