AMPylation matches BiP activity to client protein load in the endoplasmic reticulum

AMPylation matches BiP activity to client protein load in the endoplasmic reticulum

The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP affects protein folding homeostasis and the response to ER stress. Reversible inactivating covalent modification of BiP is believed to contribute to the balance between chaperones and unfolded ER proteins, but the nature of this modificati...

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Bibliographic Details
Main Authors: Steffen Preissler, Cláudia Rato, Ruming Chen, Robin Antrobus, Shujing Ding, Ian M Fearnley, David Ron
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2015-12-01
Series:eLife
Subjects:
BiP/GRP78
AMPylation
FICD/HYPE
Hsp70
chaperone
endoplasmic reticulum
Online Access:https://elifesciences.org/articles/12621

Internet

https://elifesciences.org/articles/12621

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