AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation

The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP contributes to protein folding homeostasis by engaging unfolded client proteins in a process that is tightly coupled to ATP binding and hydrolysis. The inverse correlation between BiP AMPylation and the burden of unfolded ER proteins sugge...

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Bibliographic Details
Main Authors: Steffen Preissler, Lukas Rohland, Yahui Yan, Ruming Chen, Randy J Read, David Ron
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2017-10-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/29428