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J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.
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http://dx.doi.org/10.1016/j.cstres.2023.12.002 | DOI Listing |
Nat Cell Biol
August 2025
Biozentrum, University of Basel, Basel, Switzerland.
Protein folding in the endoplasmic reticulum (ER) relies on a network of molecular chaperones that facilitates the folding and maturation of client proteins. How the ER chaperones organize in a supramolecular manner to exert their cooperativity has, however, remained unclear. Here we report the discovery of a multichaperone condensate in the ER lumen, which is formed around the chaperone PDIA6 during protein folding homeostasis.
View Article and Find Full Text PDFMol Biol Cell
September 2025
Department of Chemical Physiology and Biochemistry, Oregon Health and Science University, Portland, OR 97239.
Endosomes are a central sorting hub for membrane cargos. DNAJC13/RME-8 plays a critical role in endosomal trafficking by regulating the endosomal recycling and degradative pathways. DNAJC13 localizes to endosomes through its N-terminal Pleckstrin Homology (PH)-like domain, which binds endosomal phosphatidylinositol-3-phosphate (PI(3)P).
View Article and Find Full Text PDFJ Hum Genet
July 2025
Department of Neurology, Washington University School of Medicine, St. Louis, MO, USA.
The J-domain proteins (JDPs), or HSP40s, are essential molecular co-chaperones that, in concert with HSP70, play a pivotal role in maintaining protein homeostasis, which is particularly critical in skeletal muscle. In recent years, pathogenic variants in several JDP-encoding genes have been identified as a cause of a growing group of inherited muscle diseases, termed JDP-related myopathies. This review provides a comprehensive overview of the current understanding of the molecular genetics, clinical phenotypes, muscle pathology, and pathomechanisms of myopathies caused by mutations in DNAJB6, DNAJB4, and DNAJB2.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
College of Agriculture, Guizhou University, Guiyang 550025, Guizhou, China; Guizhou Sub-center of National Wheat Improvement Center, Guiyang 550025, China. Electronic address:
Wheat productivity is severely impacted by temperature extremes, highlighting the need to understand stress tolerance mechanisms. The Bcl-2-associated athanogene (BAG) protein family is known to regulate stress responses, yet its functional roles in wheat under heat and cold stress are not well understood. This study identified ten TaBAG genes in wheat, primarily located on chromosomes 2, 4, 5, and 7.
View Article and Find Full Text PDFbioRxiv
July 2025
Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
The heat shock response (HSR) is the major defense mechanism against proteotoxic stress in the cytosol and nucleus of eukaryotic cells. Initiation and attenuation of the response are mediated by stress-dependent regulation of heat shock transcription factors (HSFs). encodes a single HSF (Hsf1), facilitating the analysis of HSR regulation.
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