Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Mar 24;3:860404. doi: 10.3389/fragi.2022.860404

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2022 Dutta, Garcia and Higuchi-Sanabria.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

The cytosolic heat-shock response. (A) The heat-shock response (HSR) is regulated by the transcription factor, HSF-1, which contains four major structural domains: the DNA-binding domain (DBD), regulatory domain (RD), trans-activating domain (TAD), and the oligomerization domain divided into HR-A and HR-B. (B) Under basal conditions, HSF-1 is bound by regulatory proteins that prevent its activation. Upon stress, these proteins are released from HSF-1 as they are titrated away to serve as molecular chaperones to damaged proteins, allowing HSF-1 to trimerize and serve as a transcription factor to activate genes important to mitigate damage and increase survival. (C) The HSR can be communicated in a non-autonomous manner, whereby thermosensory and serotonergic neurons can communicate to peripheral tissue, including the intestine, to activate a systemic HSR and promote organismal health and lifespan.