Publication

J-domain Proteins: From Molecular Mechanisms to Diseases

2026

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.

Official source

https://infoscience.epfl.ch/entities/publication/3b458ef5-b555-495d-84e9-402fa5603230

About this result

This page is automatically generated and may contain information that is not correct, complete, up-to-date, or relevant to your search query. The same applies to every other page on this website. Please make sure to verify the information with EPFL's official sources.

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

2026

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/3b458ef5-b555-495d-84e9-402fa5603230

About this result

Related concepts (24)

Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA.

Molecular biology

Molecular biology məˈlɛkjʊlər is the study of chemical and physical structure of biological macromolecules. It is a branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. Molecular biology was first described as an approach focused on the underpinnings of biological phenomena—uncovering the structures of biological molecules as well as their interactions, and how these interactions explain observations of classical biology.

Heat shock protein

Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.