ArticleStructure (London, England : 1993)2014
Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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38 citing papers in PubMed, 60 citations in OpenAlex.
- Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- 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
- Small-Molecule FICD Inhibitors Suppress Endogenous and Pathologic FICD-Mediated Protein AMPylation.ACS chemical biology · 2025Article
- A statistical mechanics investigation of unfolded protein response across organisms.Scientific reports · 2024Article
- Loss of Fic causes progressive neurodegeneration in a Drosophila model of hereditary spastic paraplegia.Biochimica et biophysica acta. Molecular basis of disease · 2024Article
- Small molecule FICD inhibitors suppress endogenous and pathologic FICD-mediated protein AMPylation.bioRxiv : the preprint server for biology · 2024Article
- 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
- Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022Article
- The AMPylase FIC-1 modulates TGF-β signaling inFrontiers in molecular neuroscience · 2022Article
- Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.Nature communications · 2021Article
- Kinetic and structural parameters governing Fic-mediated adenylylation/AMPylation of the Hsp70 chaperone, BiP/GRP78.Cell stress & chaperones · 2021Article
- Investigation of the Detailed AMPylated Reaction Mechanism for the Huntingtin Yeast-Interacting Protein E Enzyme HYPE.International journal of molecular sciences · 2021Article
- Fic and non-Fic AMPylases: protein AMPylation in metazoans.Open biology · 2021Article
- Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.Nature communications · 2021Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Protein AMPylation, the transfer of AMP from ATP to protein targets, has been recognized as a new mechanism of host-cell disruption by some bacterial effectors that typically contain a FIC-domain. Eukaryotic genomes also encode one FIC-domain protein,HYPE, which has remained poorly characterized.Here we describe the structure of human HYPE, solved by X-ray crystallography, representing the first structure of a eukaryotic FIC-domain protein. We demonstrate that HYPE forms stable dimers with structurally and functionally integrated FIC-domains and with TPR-motifs exposed for protein-protein interactions. As HYPE also uniquely possesses a transmembrane helix, dimerization is likely to affect its positioning and function in the membrane vicinity. The low rate of auto AMPylation of the wild-type HYPE could be due to autoinhibition, consistent with the mechanism proposed for a number of putative FIC AMPylators. Our findings also provide a basis to further consider possible alternative cofactors of HYPE and distinct modes of target-recognition.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.