Study
Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
Feder, Martin E.; Hofmann, Gretchen E.
Annual Review of Physiology, 1999
Reviews the heat-shock response across organisms, covering what the proteins do, when they are produced, what producing them costs, and whether the response is used in nature as it is in the laboratory.
- Studied in
- Animalia, Plantae, Fungi, Bacteria
- Sample size
- review across kingdoms
Heat-shock proteins are molecular chaperones that bind partly unfolded proteins and either refold them or route them for disposal. The response is expensive, is regulated rather than reflexive, and organisms frequently maintain it at levels below what maximises short-term survival.
What it means
The authors' reading, and ours. Where they differ, that difference is the point.
How the authors put it
The heat-shock response is a cost–benefit compromise rather than a straightforward defence, which explains why organisms do not simply maintain it permanently.
How NatureHQ reads it
The record that turns "heat damages proteins" into something specific, and that supplies a correction NatureHQ uses on the heat page: the response has a price, which is why animals do not run it all the time and why chronic mild heat can be worse for them than an acute spike.
- A 1999 review of a large field; the molecular detail has advanced, though the cost–benefit framing has held.
- Laboratory heat shock is a sharper stimulus than most natural warming, and the two do not always produce the same response.
What this study is used for on NatureHQ
One study can inform several subjects. Here is everywhere this one is cited.
Published by: Annual ReviewsPublished in an Annual Reviews journal.
doi.org/10.1146/annurev.physiol.61.1.243
Checked against Crossref on 2026-09-28, and they agree on the title, the authors and the year.
NatureHQ summarises research in its own words and does not reproduce published text. Reviewed 2026-09-03.