Double J-domain piloting of an Hsp70 substrate

Publication date

2021-01

Authors

Aragonès Pedrola, JúliaISNI 0000000506317524
Rüdiger, S.G.D.ISNI 0000000394040769

Editors

Advisors

Supervisors

Document Type

Editorial
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License

cc_by_nc_nd

Abstract

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.

Keywords

Endoplasmic Reticulum/metabolism, HSP70 Heat-Shock Proteins/metabolism, Protein Binding, Protein Domains, Substrate Specificity

Citation

Pedrola, J A & Rüdiger, S G D 2021, 'Double J-domain piloting of an Hsp70 substrate', Journal of Biological Chemistry, vol. 296, 100717, pp. 1-2. https://doi.org/10.1016/j.jbc.2021.100717