Function, evolution, and structure of J-domain proteins

Harm H. Kampinga; Claes Andreasson; Alessandro Barducci; Michael E. Cheetham; Douglas Cyr; Cecilia Emanuelsson; Pierre Genevaux; Jason E. Gestwicki; Pierre Goloubinoff; Jaime Huerta-Cepas; Janine Kirstein; Krzysztof Liberek; Matthias P. Mayer; Kazuhiro Nagata; Nadinath B. Nillegoda; Pablo Pulido; Carlos Ramos; Paolo De los Rios; Sabine Rospert; Rina Rosenzweig; Chandan Sahi; Mikko Taipale; Bratlomiej Tomiczek; Ryo Ushioda; Jason C. Young; Richard Zimmermann; Alicja Zylicz; Maciej Zylicz; Elizabeth A. Craig; Jaroslaw Marszalek

doi:10.1007/s12192-018-0948-4

Function, evolution, and structure of J-domain proteins

Harm H. Kampinga^*, Claes Andreasson, Alessandro Barducci, Michael E. Cheetham, Douglas Cyr, Cecilia Emanuelsson, Pierre Genevaux, Jason E. Gestwicki, Pierre Goloubinoff, Jaime Huerta-Cepas, Janine Kirstein, Krzysztof Liberek, Matthias P. Mayer, Kazuhiro Nagata, Nadinath B. Nillegoda, Pablo Pulido, Carlos Ramos, Paolo De los Rios, Sabine Rospert, Rina RosenzweigChandan Sahi, Mikko Taipale, Bratlomiej Tomiczek, Ryo Ushioda, Jason C. Young, Richard Zimmermann, Alicja Zylicz, Maciej Zylicz, Elizabeth A. Craig, Jaroslaw Marszalek

^*Corresponding author for this work

Department of Chemical and Structural Biology

Research output: Contribution to journal › Review article › peer-review

106 Citations (Scopus)

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.

Original language	English
Pages (from-to)	7-15
Number of pages	9
Journal	Cell Stress & Chaperones
Volume	24
Issue number	1
Early online date	26 Nov 2018
DOIs	https://doi.org/10.1007/s12192-018-0948-4
Publication status	Published - 1 Jan 2019

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.

All Science Journal Classification (ASJC) codes

Biochemistry
Cell Biology

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Kampinga, H. H., Andreasson, C., Barducci, A., Cheetham, M. E., Cyr, D., Emanuelsson, C., Genevaux, P., Gestwicki, J. E., Goloubinoff, P., Huerta-Cepas, J., Kirstein, J., Liberek, K., Mayer, M. P., Nagata, K., Nillegoda, N. B., Pulido, P., Ramos, C., De los Rios, P., Rospert, S., ... Marszalek, J. (2019). Function, evolution, and structure of J-domain proteins. Cell Stress & Chaperones, 24(1), 7-15. https://doi.org/10.1007/s12192-018-0948-4

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title = "Function, evolution, and structure of J-domain proteins",

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.",

author = "Kampinga, {Harm H.} and Claes Andreasson and Alessandro Barducci and Cheetham, {Michael E.} and Douglas Cyr and Cecilia Emanuelsson and Pierre Genevaux and Gestwicki, {Jason E.} and Pierre Goloubinoff and Jaime Huerta-Cepas and Janine Kirstein and Krzysztof Liberek and Mayer, {Matthias P.} and Kazuhiro Nagata and Nillegoda, {Nadinath B.} and Pablo Pulido and Carlos Ramos and {De los Rios}, Paolo and Sabine Rospert and Rina Rosenzweig and Chandan Sahi and Mikko Taipale and Bratlomiej Tomiczek and Ryo Ushioda and Young, {Jason C.} and Richard Zimmermann and Alicja Zylicz and Maciej Zylicz and Craig, {Elizabeth A.} and Jaroslaw Marszalek",

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doi = "10.1007/s12192-018-0948-4",

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Kampinga, HH, Andreasson, C, Barducci, A, Cheetham, ME, Cyr, D, Emanuelsson, C, Genevaux, P, Gestwicki, JE, Goloubinoff, P, Huerta-Cepas, J, Kirstein, J, Liberek, K, Mayer, MP, Nagata, K, Nillegoda, NB, Pulido, P, Ramos, C, De los Rios, P, Rospert, S, Rosenzweig, R, Sahi, C, Taipale, M, Tomiczek, B, Ushioda, R, Young, JC, Zimmermann, R, Zylicz, A, Zylicz, M, Craig, EA & Marszalek, J 2019, 'Function, evolution, and structure of J-domain proteins', Cell Stress & Chaperones, vol. 24, no. 1, pp. 7-15. https://doi.org/10.1007/s12192-018-0948-4

TY - JOUR

T1 - Function, evolution, and structure of J-domain proteins

AU - Kampinga, Harm H.

AU - Andreasson, Claes

AU - Barducci, Alessandro

AU - Cheetham, Michael E.

AU - Cyr, Douglas

AU - Emanuelsson, Cecilia

AU - Genevaux, Pierre

AU - Gestwicki, Jason E.

AU - Goloubinoff, Pierre

AU - Huerta-Cepas, Jaime

AU - Kirstein, Janine

AU - Liberek, Krzysztof

AU - Mayer, Matthias P.

AU - Nagata, Kazuhiro

AU - Nillegoda, Nadinath B.

AU - Pulido, Pablo

AU - Ramos, Carlos

AU - De los Rios, Paolo

AU - Rospert, Sabine

AU - Rosenzweig, Rina

AU - Sahi, Chandan

AU - Taipale, Mikko

AU - Tomiczek, Bratlomiej

AU - Ushioda, Ryo

AU - Young, Jason C.

AU - Zimmermann, Richard

AU - Zylicz, Alicja

AU - Zylicz, Maciej

AU - Craig, Elizabeth A.

AU - Marszalek, Jaroslaw

PY - 2019/1/1

Y1 - 2019/1/1

N2 - 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.

AB - 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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U2 - 10.1007/s12192-018-0948-4

DO - 10.1007/s12192-018-0948-4

M3 - Review article

SN - 1355-8145

VL - 24

SP - 7

EP - 15

JO - Cell Stress & Chaperones

JF - Cell Stress & Chaperones

IS - 1

ER -

Function, evolution, and structure of J-domain proteins

Abstract

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