An oligomeric state-dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP.
FICD
AMPylation
BiP
deAMPylation
endoplasmic reticulum
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
04 10 2019
04 10 2019
Historique:
received:
04
04
2019
revised:
25
07
2019
accepted:
26
07
2019
pubmed:
19
9
2019
medline:
7
1
2020
entrez:
19
9
2019
Statut:
ppublish
Résumé
AMPylation is an inactivating modification that alters the activity of the major endoplasmic reticulum (ER) chaperone BiP to match the burden of unfolded proteins. A single ER-localised Fic protein, FICD (HYPE), catalyses both AMPylation and deAMPylation of BiP. However, the basis for the switch in FICD's activity is unknown. We report on the transition of FICD from a dimeric enzyme, that deAMPylates BiP, to a monomer with potent AMPylation activity. Mutations in the dimer interface, or of residues along an inhibitory pathway linking the dimer interface to the enzyme's active site, favour BiP AMPylation in vitro and in cells. Mechanistically, monomerisation relieves a repressive effect allosterically propagated from the dimer interface to the inhibitory Glu234, thereby permitting AMPylation-competent binding of MgATP. Moreover, a reciprocal signal, propagated from the nucleotide-binding site, provides a mechanism for coupling the oligomeric state and enzymatic activity of FICD to the energy status of the ER.
Identifiants
pubmed: 31531998
doi: 10.15252/embj.2019102177
pmc: PMC6826200
doi:
Substances chimiques
Endoplasmic Reticulum Chaperone BiP
0
Heat-Shock Proteins
0
Membrane Proteins
0
FICD protein, human
EC 2.7.7.-
Nucleotidyltransferases
EC 2.7.7.-
Banques de données
PDB
['6I7G', '6I7H', '6I7I', '6I7J', '6I7K', '6I7L']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e102177Subventions
Organisme : Wellcome Trust
ID : 209407/Z/17/Z
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U105184326
Pays : United Kingdom
Informations de copyright
© 2019 The Authors. Published under the terms of the CC BY 4.0 license.
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