Plant Heat Shock Protein Hsp90 enhances stress resistance through integrating protein quality control, chloroplast protection, hormone signal network, and immune defense

© The Author(s) 2025. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For commercial re-use, please contact reprintsoup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink serv...

Description complète

Détails bibliographiques
Publié dans:Journal of experimental botany. - 1985. - (2025) vom: 13. Okt.
Auteur principal: Wu, Jieting (Auteur)
Autres auteurs: Li, Yuxin, Yin, Haoran, Zhao, Lei, Xu, Chengbin, Fu, Xiaofan, Shang, Jing, Liu, Shuhan, Guo, Haijuan, Ma, Fang
Format: Article en ligne
Langue:English
Publié: 2025
Accès à la collection:Journal of experimental botany
Sujets:Journal Article Biotic interactions Hormone Hsp90 (Heat shock protein 90) Immune Plant cell Stress
Description
Résumé:© The Author(s) 2025. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For commercial re-use, please contact reprintsoup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.
Given the groundbreaking progress in identifying unique functions of plant Hsp90 in stress responses in recent years, and the absence of systematic integration of these new mechanisms in protein quality control, hormone network regulation, chloroplast protection, and immune defense in existing reviews, this article aims to fill this gap. Recent studies have revealed four key mechanisms: (1) Hsp90 forms complexes with E3 ligases to promote polyubiquitination of heat-induced protein aggregates, cooperating with the 26S proteasome for clearance, a pathway hijacked by viruses; (2) Hsp90 stabilizes auxin receptor TIR1, reconstructs root auxin gradients via polarized PIN1, activates ABA biosynthesis, and enhances insect resistance through JA signaling; (3) Hsp90C maintains photosystem renewal, protects chloroplast DNA via CND1 translocation, and stabilizes thylakoid proteins via its CTE domain; (4) Hsp90 escorts CERK1 to initiate PTI, activates NLRs for ETI, and interacts with ATG8 to enhance autophagic pathogen clearance. This review integrates key new discoveries since 2012, and identifies core research gaps to address, namely regulation of Hsp90 abundance "optimal threshold", its combined stress response mechanism, transformation of knowledge from model plants to major food crops, and provides a clear direction framework for subsequent research
Description:Date Revised 13.10.2025
published: Print-Electronic
Citation Status Publisher
ISSN:1460-2431
DOI:10.1093/jxb/eraf447