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Department of Applied Physics Experim... 1 Department of Physiology and Pharmaco... 1 Department of Physiology and Pharmaco... 1 Institute of Chemistry The Hebrew Uni... 1 Science for Life Laboratory Departmen... 1 Science for Life Laboratory Departmen... 1 Single Technologies AB SE 114 28 Stoc... 1
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Department of Applied Physics Experim... 1 Department of Physiology and Pharmaco... 1 Department of Physiology and Pharmaco... 1 Institute of Chemistry The Hebrew Uni... 1 Science for Life Laboratory Departmen... 1 Science for Life Laboratory Departmen... 1 Single Technologies AB SE 114 28 Stoc... 1
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Free Medical Journals od 2010
Nature Open Access od 2010-12-01
PubMed Central od 2012
Europe PubMed Central od 2012
ProQuest Central od 2010-01-01
Open Access Digital Library od 2015-01-01
Open Access Digital Library od 2015-01-01
Medline Complete (EBSCOhost) od 2012-11-01
Health & Medicine (ProQuest) od 2010-01-01
ROAD: Directory of Open Access Scholarly Resources od 2010
PubMed
28790300
DOI
10.1038/s41467-017-00253-9
Knihovny.cz E-zdroje
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 α-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 agonist-dependent dynamics of dimers as an intrinsic process of receptor activation extends our understanding of Class F and other dimerizing GPCRs, offering novel targets for dimer-interfering small molecules.Frizzled 6 (FZD6) is a G protein-coupled receptor (GPCR) involved in several cellular processes. Here, the authors use live cell imaging and spectroscopy to show that FZD6 forms dimers, whose association is regulated by WNT proteins and that dimer dissociation is crucial for FZD6 signaling.
- MeSH
- dimerizace MeSH
- frizzled receptory metabolismus MeSH
- HEK293 buňky MeSH
- lidé MeSH
- protein Wnt 5a metabolismus MeSH
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- lidé MeSH
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- práce podpořená grantem MeSH
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