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Structural and molecular basis of ZNRF3/RNF43 transmembrane ubiquitin ligase inhibition by the Wnt agonist R-spondin

DOI: 10.1038/ncomms3787 DOI Help
PMID: 24225776 PMID Help

Authors: Matthias Zebisch (University of Oxford) , Yang Xu (Boston Children’s Hospital, Harvard Medical School) , Christos Krastev (University of Oxford) , Bryan T. Macdonald (Boston Children’s Hospital, Harvard Medical School) , Maorong Chen (Boston Children’s Hospital, Harvard Medical School) , Robert J. C. Gilbert (University of Oxford) , Xi He (Boston Children’s Hospital, Harvard Medical School) , Edith Jones (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 4

State: Published (Approved)
Published: November 2013
Diamond Proposal Number(s): 8423

Open Access Open Access

Abstract: The four R-spondin (Rspo) proteins are secreted agonists of Wnt signalling in vertebrates, functioning in embryogenesis and adult stem cell biology. Through ubiquitination and degradation of Wnt receptors, the transmembrane E3 ubiquitin ligase ZNRF3 and related RNF43 antagonize Wnt signalling. Rspo ligands have been reported to inhibit the ligase activity through direct interaction with ZNRF3 and RNF43

Journal Keywords: DNA-Binding; Dimerization; Humans; Mice; Oncogene; Protein; Receptors; G-Protein-Coupled; Thrombospondins; Ubiquitin-Protein; Wnt; Xenopus; Zebrafish

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 18/12/2013 09:30

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