Abstract
Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.
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Funding
The organizers would like to thank the Cell Stress Society International (CSSI) for their financial support of the workshop. We also thank the Rector of the University of Gdansk, the Dean of the Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, and The University Medical Center Groningen for financial support. During organization of this workshop JM was supported by Polish National Science Center Grant DEC-2012/06/A/NZ1/00002.
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Kampinga, H.H., Andreasson, C., Barducci, A. et al. Function, evolution, and structure of J-domain proteins. Cell Stress and Chaperones 24, 7–15 (2019). https://doi.org/10.1007/s12192-018-0948-4
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DOI: https://doi.org/10.1007/s12192-018-0948-4