| Literature DB >> 30478692 |
Harm H Kampinga1, Claes Andreasson2, Alessandro Barducci3, Michael E Cheetham4, Douglas Cyr5, Cecilia Emanuelsson6, Pierre Genevaux7, Jason E Gestwicki8, Pierre Goloubinoff9, Jaime Huerta-Cepas10, Janine Kirstein11, Krzysztof Liberek12, Matthias P Mayer13, Kazuhiro Nagata14, Nadinath B Nillegoda13,15, Pablo Pulido16, Carlos Ramos17, Paolo De Los Rios18, Sabine Rospert19, Rina Rosenzweig20, Chandan Sahi21, Mikko Taipale22, Bratłomiej Tomiczek12, Ryo Ushioda14, Jason C Young23, Richard Zimmermann24, Alicja Zylicz25, Maciej Zylicz25, Elizabeth A Craig26, Jaroslaw Marszalek12.
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.Entities:
Keywords: 8-stranded β-sandwich domain (SBDβ); Heat shock protein 70 (Hsp70); J-domain proteins (JDPs)
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Year: 2018 PMID： 30478692 PMCID： PMC6363617 DOI： 10.1007/s12192-018-0948-4
Source DB: PubMed Journal: Cell Stress Chaperones ISSN： 1355-8145 Impact factor: 3.667