Wiring of cellular proteostasis by J-domain proteins

Matthias P. Mayer

doi:10.1016/j.cstres.2026.100191

May 1, 2026Cell Stress and ChaperonesOpen Access

Wiring of cellular proteostasis by J-domain proteins

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Key Points

This research aims to illuminate the central role of J-domain proteins in the chaperone network, particularly their decision-making function relative to Hsp70s.
Analyzed the interactions between J-domain proteins and Hsp70 heat shock proteins.
Investigated the role of JDPs in regulating the ATPase activity of Hsp70s with bound substrate.
J-domain proteins are key decision-makers within the Hsp70 network.
JDPs significantly influence the ATPase activity of Hsp70s, refining our understanding of protein folding processes.
The study redefines the conventional view, highlighting JDPs as central components rather than mere accessories.

Implication

Reveals the critical role of J-domain proteins in regulating heat shock protein activity, influencing proteostasis.

Abstract

Originally J-domain proteins (JDPs) were viewed as accessory co-chaperones of 70 kDa heat shock proteins (Hsp70s), the actual chaperones, stimulating ATPase activity of Hsp70s when a protein substrate is bound. This view apparently underestimates the role of JDPs as most of the decisions within the Hsp70 network seems to be taken at the level of JDPs. The JDPs are so to speak the brain and the Hsp70s are the muscles of this chaperone network.

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Cite This Study

Matthias P. Mayer (2026) studied this question.

synapsesocial.com/papers/6a12959d48a0ea1665671b75 https://doi.org/10.1016/j.cstres.2026.100191

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Wiring of cellular proteostasis by J-domain proteins

Key Points

Implication

Abstract

Discussion

Cite This Study

Wiring of cellular proteostasis by J-domain proteins

Key Points

Implication

Abstract

Discussion

Cite This Study

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