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Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling
Karolinska Inst, Sect Receptor Biol & Signaling, Dept Physiol & Pharmacol, S-17177 Stockholm, Sweden..
Karolinska Inst, Sect Receptor Biol & Signaling, Dept Physiol & Pharmacol, S-17177 Stockholm, Sweden..
Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, SE-10691 Stockholm, Sweden..
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Computational Biology and Bioinformatics. Uppsala University, Science for Life Laboratory, SciLifeLab.
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2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, article id 226Article in journal (Refereed) Published
Abstract [en]

G protein-coupled receptors (GPCRs) constitute the largest family of cell surface receptors. They can exist and act as dimers, but the requirement of dimers for agonist-induced signal initiation and structural dynamics remains largely unknown. Frizzled 6 (FZD6) is a member of Class F GPCRs, which bind WNT proteins to initiate signaling. Here, we show that FZD6 dimerizes and that the dimer interface of FZD6 is formed by the transmembrane a-helices four and five. Most importantly, we present the agonist-induced dissociation/re-association of a GPCR dimer through the use of live cell imaging techniques. Further analysis of a dimerization-impaired FZD6 mutant indicates that dimer dissociation is an integral part of FZD6 signaling to extracellular signal-regulated kinases1/2. The discovery of agonistdependent dynamics of dimers as an intrinsic process of receptor activation extends our understanding of Class F and other dimerizing GPCRs, offering novel targets for dimerinterfering small molecules.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017. Vol. 8, article id 226
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Biological Sciences
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URN: urn:nbn:se:uu:diva-334041DOI: 10.1038/s41467-017-00253-9ISI: 000407198800015PubMedID: 28790300OAI: oai:DiVA.org:uu-334041DiVA, id: diva2:1159015
Available from: 2017-11-21 Created: 2017-11-21 Last updated: 2017-11-29Bibliographically approved

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