Double J-domain piloting of an Hsp70 substrate.

Autor:	Aragonès Pedrola J; Cellular Protein Chemistry, Bijvoet Centre for Biomolecular Research, Utrecht University, Utrecht, The Netherlands; Science for Life, Utrecht University, Utrecht, The Netherlands., Rüdiger SGD; Cellular Protein Chemistry, Bijvoet Centre for Biomolecular Research, Utrecht University, Utrecht, The Netherlands; Science for Life, Utrecht University, Utrecht, The Netherlands. Electronic address: s.g.d.rudiger@uu.nl.
Jazyk:	angličtina
Zdroj:	The Journal of biological chemistry [J Biol Chem] 2021 Jan-Jun; Vol. 296, pp. 100717. Date of Electronic Publication: 2021 Apr 27.
DOI:	10.1016/j.jbc.2021.100717
Abstrakt:	Heat shock 70 kDa protein (Hsp70) chaperones play a crucial role in the biogenesis of tail-anchored proteins (TAs), starting a downstream cascade to the endoplasmic reticulum (ER) via the guided-entry-of-tail-anchored protein (GET) pathway. J-domain proteins (JDPs) are generally known to assist Hsp70s, but their specific role in TA targeting remains unclear. Cho et al. now identify two separate functions for JDPs in the process, in the initial capture of the TA and the transfer into the GET pathway. These data suggest that several Hsp70 cycles could be involved at distinct steps during protein maturation. Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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