J-domain proteins: from molecular mechanisms to diseases

J-domain proteins (JDPs) are known to drive the functional specificity of Hsp70 chaperone machines. Here we report on the latest findings presented at the third international JDP workshop held in 2025 in Gdansk, Poland. Investigators from many different disciplines, including structural biology, genetics, chemical biology, translational research, computational sciences, and biophysics, took part in the meeting. This article includes short summaries of the seminars presented by many of the speakers, which provided exciting new insights into the chaperone-dependent and chaperone-independent functions of JDPs, some of which go beyond Hsp70-dependent functions. We also provide a revised classification of members of the (human) JDP family that emerged from open discussion at the meeting. This workshop continues to serve as the premier venue for discussions of JDP evolution, structure, function, and roles in health, aging, and disease.

Institutions

Publication Details

Journal
Cell Stress and Chaperones
Published
2025-12-19
DOI
https://doi.org/10.1016/j.cstres.2025.100142
Primary Topic
Heat shock proteins research
Type
article
Field-Weighted Citation Impact
0.00
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article

J-domain proteins: from molecular mechanisms to diseases

Cell Stress and Chaperones
Heat shock proteins research
article

J-domain proteins: from molecular mechanisms to diseases

article en

Abstract

J-domain proteins (JDPs) are known to drive the functional specificity of Hsp70 chaperone machines. Here we report on the latest findings presented at the third international JDP workshop held in 2025 in Gdansk, Poland. Investigators from many different disciplines, including structural biology, genetics, chemical biology, translational research, computational sciences, and biophysics, took part in the meeting. This article includes short summaries of the seminars presented by many of the speakers, which provided exciting new insights into the chaperone-dependent and chaperone-independent functions of JDPs, some of which go beyond Hsp70-dependent functions. We also provide a revised classification of members of the (human) JDP family that emerged from open discussion at the meeting. This workshop continues to serve as the premier venue for discussions of JDP evolution, structure, function, and roles in health, aging, and disease.

Cell Stress and ChaperonesVol. 31(1)
University of North Carolina at Chapel Hill (US), Goethe University Frankfurt (DE), Centre National de la Recherche Scientifique (FR), University Medical Center Groningen (NL), University of Wisconsin–Madison (US), Radboud University Nijmegen (NL), University of Liverpool (GB), Inserm (FR), University of Freiburg (DE), Stockholm University (SE), Kyoto Sangyo University (JP), University of Calgary (CA), University of Pittsburgh (US), Technion – Israel Institute of Technology (IL), University of California, San Francisco (US), University of Toronto (CA), Lund University (SE), Washington University in St. Louis (US), Aix-Marseille Université (FR), Heidelberg University (DE), The Francis Crick Institute (GB), Radboud University Medical Center (NL), Indian Institute of Science Education and Research, Bhopal (IN), University of Gdańsk (PL), Centre de Biologie Structurale (FR), Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) (DE), Institute of Ophthalmology (MX), Délégation Provence et Corse (FR), Max Planck Institute of Neurobiology (DE), Laboratoire de Microbiologie et Génétique Moléculaires (FR), William Harvey Research Institute (GB), DKFZ-ZMBH Alliance (DE), University College London (GB), École Polytechnique Fédérale de Lausanne (CH), Weizmann Institute of Science (IL), Ludwig-Maximilians-Universität München (DE), The University of Texas Southwestern Medical Center (US), Nanjing University (CN), The University of Notre Dame Australia (AU), University of Lausanne (CH)
Partnerships for the goals
Openalex Percentile: Top 37%
Heat shock proteins research
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