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Function, evolution, and structure of J-domain proteins

Kampinga, Harm H.; Andreasson, Claes; Barducci, Alessandro; Cheetham, Michael E.; Cyr, Douglas; Emanuelsson, Cecilia LU ; Genevaux, Pierre; Gestwicki, Jason E.; Goloubinoff, Pierre and Huerta-Cepas, Jaime, et al. (2018) In Cell Stress and Chaperones
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... (More)

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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@article{be45b0cb-997f-44a6-b9ca-4c1c625e728d,
  abstract     = {<p>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.</p>},
  author       = {Kampinga, Harm H. and Andreasson, Claes and Barducci, Alessandro and Cheetham, Michael E. and Cyr, Douglas and Emanuelsson, Cecilia and Genevaux, Pierre and Gestwicki, Jason E. and Goloubinoff, Pierre and Huerta-Cepas, Jaime and Kirstein, Janine and Liberek, Krzysztof and Mayer, Matthias P. and Nagata, Kazuhiro and Nillegoda, Nadinath B. and Pulido, Pablo and Ramos, Carlos and De los Rios, Paolo and Rospert, Sabine and Rosenzweig, Rina and Sahi, Chandan and Taipale, Mikko and Tomiczek, Bratłomiej and Ushioda, Ryo and Young, Jason C. and Zimmermann, Richard and Zylicz, Alicja and Zylicz, Maciej and Craig, Elizabeth A. and Marszalek, Jaroslaw},
  issn         = {1355-8145},
  keyword      = {8-stranded β-sandwich domain (SBDβ),Heat shock protein 70 (Hsp70),J-domain proteins (JDPs)},
  language     = {eng},
  month        = {11},
  publisher    = {Churchill Livingstone},
  series       = {Cell Stress and Chaperones},
  title        = {Function, evolution, and structure of J-domain proteins},
  url          = {http://dx.doi.org/10.1007/s12192-018-0948-4},
  year         = {2018},
}