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Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
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Number of Authors: 11
2017 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 8, 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
2017. Vol. 8, 226
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Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-147099DOI: 10.1038/s41467-017-00253-9ISI: 000407198800015PubMedID: 28790300OAI: oai:DiVA.org:su-147099DiVA: diva2:1148567
Available from: 2017-10-11 Created: 2017-10-11 Last updated: 2017-11-29Bibliographically approved

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