A new study shows that TPR-containing co-chaperones of HSP70 and HSP90 help plants fine-tune hormone signaling, protein quality control, and defense, with evidence for both conserved and plant-specific mechanisms.
A joint study published in the Journal of Experimental Botany by researchers from the CBGP and IBMCP spotlights different plant Tetratricopeptide repeat (TPR)-containing co-chaperones as major regulators of proteostasis, the system that keeps proteins functional and balanced inside cells. The authors show that these co-chaperones help the central chaperones HSP70 and HSP90 select, fold, stabilize, and traffic important client proteins. The review highlights three major examples: RPAP3, which is linked to assembly of large cellular complexes; HOP, which helps coordinate hormone responses, heat adaptation, and stress protection; and SGT1, a central regulator of disease resistance and signaling. Together, the evidence suggests these proteins form a regulatory node that helps plants adapt growth, stress resistance and defense to changing environmental conditions.
Original Paper: Palacios-Abella, A., Tello-Rodríguez, S., Castellano, M.M., Alabadí, D. 2026. TPR domain-containing co-chaperones of HSP70 and HSP90 in plants. Journal of Experimental Botany erag118. DOI: 10.1093/jxb/erag118
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