ArticleNature communications2021
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Article
- The toxin-antitoxin complex Fic-1-AntF functions as a deAMPylase that regulates the activity of DNA gyrase.mLife · 2026Article
- Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Increased FICD-mediated protein AMPylation triggers conserved endoplasmic reticulum stress signaling across species.Cell stress & chaperones · 2026Article
- AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026Review
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- The rise of AMPylation: from bacterial beginnings to modern implications in health and disease.Biochemical Society transactions · 2025Review
- The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- FICD (FIC Domain Protein Adenylyl Transferase) Deficiency Protects Mice From Hypertrophy-Induced Heart Failure and Promotes BiP (Binding Immunoglobulin Protein) -Mediated Activation of the Unfolded Protein Response and Endoplasmic Reticulum-Selective Autophagy in Cardiomyocytes.Journal of the American Heart Association · 2025Article
- Loss of FIC-1-mediated AMPylation activates the UPRER and upregulates cytosolic HSP70 chaperones to suppress polyglutamine toxicity.PLoS genetics · 2025Article
- Small-Molecule FICD Inhibitors Suppress Endogenous and Pathologic FICD-Mediated Protein AMPylation.ACS chemical biology · 2025Article
- Predictive Value and Immunological Role of the HSPA5 Gene in Cervical Cancer.Biochemical genetics · 2025Article
- FicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Small molecule FICD inhibitors suppress endogenous and pathologic FICD-mediated protein AMPylation.bioRxiv : the preprint server for biology · 2024Article
- The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3.Communications biology · 2023Article
- Infancy-onset diabetes caused by de-regulated AMPylation of the human endoplasmic reticulum chaperone BiP.EMBO molecular medicine · 2023Article
- AMPylation and Endoplasmic Reticulum Protein Folding Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation.Angewandte Chemie (International ed. in English) · 2023Article
- Catalytic deAMPylation in AMPylation-inhibitory/assistant forms of FICD protein.Frontiers in chemistry · 2023Article
- A secreted effector with a dual role as a toxin and as a transcriptional factor.Nature communications · 2022Article
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Abstract
The endoplasmic reticulum (ER) Hsp70 chaperone BiP is regulated by AMPylation, a reversible inactivating post-translational modification. Both BiP AMPylation and deAMPylation are catalysed by a single ER-localised enzyme, FICD. Here we present crystallographic and solution structures of a deAMPylation Michaelis complex formed between mammalian AMPylated BiP and FICD. The latter, via its tetratricopeptide repeat domain, binds a surface that is specific to ATP-state Hsp70 chaperones, explaining the exquisite selectivity of FICD for BiP's ATP-bound conformation both when AMPylating and deAMPylating Thr518. The eukaryotic deAMPylation mechanism thus revealed, rationalises the role of the conserved Fic domain Glu234 as a gatekeeper residue that both inhibits AMPylation and facilitates hydrolytic deAMPylation catalysed by dimeric FICD. These findings point to a monomerisation-induced increase in Glu234 flexibility as the basis of an oligomeric state-dependent switch between FICD's antagonistic activities, despite a similar mode of engagement of its two substrates - unmodified and AMPylated BiP.
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