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Function, evolution, and structure of J-domain proteins

Kampinga, HH; Andreasson, C; Barducci, A; Cheetham, ME; Cyr, D; Emanuelsson, C; Genevaux, P; ... Marszalek, J; + view all (2019) Function, evolution, and structure of J-domain proteins. Cell Stress and Chaperones , 24 (1) pp. 7-15. 10.1007/s12192-018-0948-4. Green open access

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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.

Type: Article
Title: Function, evolution, and structure of J-domain proteins
Location: Netherlands
Open access status: An open access version is available from UCL Discovery
DOI: 10.1007/s12192-018-0948-4
Publisher version: https://doi.org/10.1007/s12192-018-0948-4
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Heat shock protein 70 (Hsp70), J-domain proteins (JDPs), 8-stranded β-sandwich domain (SBDβ)
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology
URI: https://discovery.ucl.ac.uk/id/eprint/10063228
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