FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP
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Protein folding homeostasis in the endoplasmic reticulum (ER) is defended by an unfolded protein response that matches ER chaperone capacity to the burden of unfolded proteins. As levels of unfolded proteins decline, a metazoan-specific FIC-domain-containing ER-localized enzyme (FICD) rapidly inactivates the major ER chaperone BiP by AMPylating T518. Here we show that the single catalytic domain of FICD can also release the attached AMP, restoring functionality to BiP. Consistent with a role for endogenous FICD in de-AMPylating BiP, FICD
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1545-9985
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Wellcome Trust (200848/Z/16/Z)
Wellcome Trust (100140/Z/12/Z)