Abstract 2444 The role of the glycine-rich region of class B J-domain proteins in the interaction with Hsp70

Molecular chaperone systems, composed of Hsp70 and J-domain proteins (JDPs), are fundamental for the quality control of virtually all other proteins in the cell. In the current model, the more structurally and functionally diverse JDPs act as cochaperones, recruiting a multifunctional molecular chaperone, Hsp70, to support various biological activities. Among the three classes of JDPs, class B representatives are unique, not only due to their essential yet unknown function but also because of their ability to recruit Hsp70 for fragmentation of amylogenic-like protein fibrils found in human neurodegenerative diseases such as Alzheimer's or Parkinson's.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109998
Primary Topic
Heat shock proteins research
Type
article
Field-Weighted Citation Impact
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article

Abstract 2444 The role of the glycine-rich region of class B J-domain proteins in the interaction with Hsp70

Szymon J. Ciesielski, Linden Gledhill, Joy Boktor
Journal of Biological Chemistry
Heat shock proteins research
article

Abstract 2444 The role of the glycine-rich region of class B J-domain proteins in the interaction with Hsp70

Szymon J. Ciesielski, Linden Gledhill, Joy Boktor
article en

Abstract

Molecular chaperone systems, composed of Hsp70 and J-domain proteins (JDPs), are fundamental for the quality control of virtually all other proteins in the cell. In the current model, the more structurally and functionally diverse JDPs act as cochaperones, recruiting a multifunctional molecular chaperone, Hsp70, to support various biological activities. Among the three classes of JDPs, class B representatives are unique, not only due to their essential yet unknown function but also because of their ability to recruit Hsp70 for fragmentation of amylogenic-like protein fibrils found in human neurodegenerative diseases such as Alzheimer's or Parkinson's.

Journal of Biological ChemistryVol. 301(5)
University of North Carolina at Chapel Hill (US)
Openalex Percentile: Top 88%
Heat shock proteins research
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