PETERSEN, J., SC WRIGHT, D. RODRIGUEZ, P. MATRICON, N. LAHAV, A. VROMEN, A. FRIEDLER, J. STROMQVIST, S. WENNMALM, J. CARLSSON and Gunnar SCHULTE. Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling. Nature Communications. London: Nature Publishing Group, 2017, vol. 8, August, p. 1-15. ISSN 2041-1723. Available from: https://dx.doi.org/10.1038/s41467-017-00253-9. |
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@article{1411800, author = {Petersen, J. and Wright, SC and Rodriguez, D. and Matricon, P. and Lahav, N. and Vromen, A. and Friedler, A. and Stromqvist, J. and Wennmalm, S. and Carlsson, J. and Schulte, Gunnar}, article_location = {London}, article_number = {August}, doi = {http://dx.doi.org/10.1038/s41467-017-00253-9}, keywords = {CROSS-CORRELATION SPECTROSCOPY; MOLECULAR-DYNAMICS SIMULATIONS; A GPCR DIMERS; FRIZZLED 6; ADRENERGIC-RECEPTOR; CONSTANT-PRESSURE; COMPLEX; BINDING; OLIGOMERIZATION; DIMERIZATION}, language = {eng}, issn = {2041-1723}, journal = {Nature Communications}, title = {Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling}, volume = {8}, year = {2017} }
TY - JOUR ID - 1411800 AU - Petersen, J. - Wright, SC - Rodriguez, D. - Matricon, P. - Lahav, N. - Vromen, A. - Friedler, A. - Stromqvist, J. - Wennmalm, S. - Carlsson, J. - Schulte, Gunnar PY - 2017 TI - Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling JF - Nature Communications VL - 8 IS - August SP - 1-15 EP - 1-15 PB - Nature Publishing Group SN - 20411723 KW - CROSS-CORRELATION SPECTROSCOPY KW - MOLECULAR-DYNAMICS SIMULATIONS KW - A GPCR DIMERS KW - FRIZZLED 6 KW - ADRENERGIC-RECEPTOR KW - CONSTANT-PRESSURE KW - COMPLEX KW - BINDING KW - OLIGOMERIZATION KW - DIMERIZATION N2 - 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. ER -
PETERSEN, J., SC WRIGHT, D. RODRIGUEZ, P. MATRICON, N. LAHAV, A. VROMEN, A. FRIEDLER, J. STROMQVIST, S. WENNMALM, J. CARLSSON and Gunnar SCHULTE. Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling. \textit{Nature Communications}. London: Nature Publishing Group, 2017, vol.~8, August, p.~1-15. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-017-00253-9.
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