| 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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