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Cell Stress Chaperones. 2018 Nov 26. doi: 10.1007/s12192-018-0948-4. [Epub ahead of print]

Function, evolution, and structure of J-domain proteins.

Author information

1
Department of Cell Biology, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. h.h.kampinga@umcg.nl.
2
Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, SE-106 91, Stockholm, Sweden.
3
Inserm, U1054, CNRS, UMR 5048, Centre de Biochimie Structurale, Universite de Montpellier, Montpellier, France.
4
UCL Institute of Ophthalmology, London, UK.
5
University of North Carolina, Chapel Hill, NC, USA.
6
Center for Molecular Protein Sciences, CMPS, Dept. Biochemistry and Structural Biology, Lund University, Lund, Sweden.
7
Laboratoire de Microbiologie et de Génétique Moléculaires, Centre de Biologie Intégrative (CBI), CNRS-Université de Toulouse, 118 route de Narbonne, 31062, Toulouse Cedex 9, France.
8
Institute for Neurodegenerative Diseases, University of California, San Francisco, CA, USA.
9
Department of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.
10
European Molecular Biology Laboratory, Heidelberg, Germany.
11
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Berlin, Germany.
12
Intercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Abrahama 58, 80-307, Gdansk, Poland.
13
Center for Molecular Biology of Heidelberg University (ZMBH), Heidelberg, Germany.
14
Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, 603-8555, Japan.
15
Australian Regenerative Medicine Institute (ARMI), Monash University, 15 Innovative Walk, Wellington Road, Clayton, VIC, 3800, Australia.
16
Plant Molecular Biology, Faculty of Biology, Ludwig-Maximilians-University, Planegg-Martinsried, 82152, Munich, Germany.
17
Institute of Chemistry, University of Campinas UNICAMP, Campinas, SP, Brazil.
18
EPFL SB IPHYS LBS BSP 723 (Cubotron UNIL), Rte de la Sorge, CH-1015, Lausanne, Switzerland.
19
Institut fur Biochemie und Molekularbiologie, Universitat Freiburg, Freiburg, Germany.
20
Weizmann Institute of Science, Rehovot, Israel.
21
Indian Institute of Science Education and Research Bhopal, Bhauri Bhopal, Madhya Pradesh, 462 066, India.
22
Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, University of Toronto, Toronto, Canada.
23
Department of Biochemistry, McGill University, Montreal, Canada.
24
Medical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
25
International Institute of Molecular and Cell Biology, Warsaw, Poland.
26
Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.

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.

KEYWORDS:

8-stranded β-sandwich domain (SBDβ); Heat shock protein 70 (Hsp70); J-domain proteins (JDPs)

PMID:
30478692
DOI:
10.1007/s12192-018-0948-4

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