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

Research output: Contribution to journalReview articlepeer-review

24 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 languageEnglish
Pages (from-to)7-15
Number of pages9
JournalCell stress & chaperones
Volume24
Issue number1
DOIs
Publication statusPublished - Jan-2019

Keywords

  • Heat shock protein 70 (Hsp70)
  • J-domain proteins (JDPs)
  • 8-stranded -sandwich domain (SBD)
  • HEAT-SHOCK PROTEINS
  • ENDOPLASMIC-RETICULUM
  • HSP70 CHAPERONE
  • MOLECULAR CHAPERONES
  • DNAJ
  • SUBSTRATE
  • RELEASE
  • HSC70
  • AGGREGATION
  • SUPPRESSION

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