Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics. / Møller, Thor C; Hottin, Jerome; Clerté, Caroline; Zwier, Jurriaan M; Durroux, Thierry; Rondard, Philippe; Prézeau, Laurent; Royer, Catherine A; Pin, Jean-Philippe; Margeat, Emmanuel; Kniazeff, Julie.

In: Scientific Reports, Vol. 8, No. 1, 10.07.2018, p. 10414.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Møller, TC, Hottin, J, Clerté, C, Zwier, JM, Durroux, T, Rondard, P, Prézeau, L, Royer, CA, Pin, J-P, Margeat, E & Kniazeff, J 2018, 'Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics', Scientific Reports, vol. 8, no. 1, pp. 10414. https://doi.org/10.1038/s41598-018-28682-6

APA

Møller, T. C., Hottin, J., Clerté, C., Zwier, J. M., Durroux, T., Rondard, P., Prézeau, L., Royer, C. A., Pin, J-P., Margeat, E., & Kniazeff, J. (2018). Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics. Scientific Reports, 8(1), 10414. https://doi.org/10.1038/s41598-018-28682-6

Vancouver

Møller TC, Hottin J, Clerté C, Zwier JM, Durroux T, Rondard P et al. Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics. Scientific Reports. 2018 Jul 10;8(1):10414. https://doi.org/10.1038/s41598-018-28682-6

Author

Møller, Thor C ; Hottin, Jerome ; Clerté, Caroline ; Zwier, Jurriaan M ; Durroux, Thierry ; Rondard, Philippe ; Prézeau, Laurent ; Royer, Catherine A ; Pin, Jean-Philippe ; Margeat, Emmanuel ; Kniazeff, Julie. / Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics. In: Scientific Reports. 2018 ; Vol. 8, No. 1. pp. 10414.

Bibtex

@article{6490cc1053e34bfb9b019d930cab2f1c,
title = "Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics",
abstract = "G protein coupled receptors (GPCRs) play essential roles in intercellular communication. Although reported two decades ago, the assembly of GPCRs into dimer and larger oligomers in their native environment is still a matter of intense debate. Here, using number and brightness analysis of fluorescently labeled receptors in cultured hippocampal neurons, we confirm that the metabotropic glutamate receptor type 2 (mGlu2) is a homodimer at expression levels in the physiological range, while heterodimeric GABAB receptors form larger complexes. Surprisingly, we observed the formation of larger mGlu2 oligomers upon both activation and inhibition of the receptor. Stabilizing the receptor in its inactive conformation using biochemical constraints also led to the observation of oligomers. Following our recent observation that mGlu receptors are in constant and rapid equilibrium between several states under basal conditions, we propose that this structural heterogeneity limits receptor oligomerization. Such assemblies are expected to stabilize either the active or the inactive state of the receptor.",
author = "M{\o}ller, {Thor C} and Jerome Hottin and Caroline Clert{\'e} and Zwier, {Jurriaan M} and Thierry Durroux and Philippe Rondard and Laurent Pr{\'e}zeau and Royer, {Catherine A} and Jean-Philippe Pin and Emmanuel Margeat and Julie Kniazeff",
year = "2018",
month = jul,
day = "10",
doi = "10.1038/s41598-018-28682-6",
language = "English",
volume = "8",
pages = "10414",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics

AU - Møller, Thor C

AU - Hottin, Jerome

AU - Clerté, Caroline

AU - Zwier, Jurriaan M

AU - Durroux, Thierry

AU - Rondard, Philippe

AU - Prézeau, Laurent

AU - Royer, Catherine A

AU - Pin, Jean-Philippe

AU - Margeat, Emmanuel

AU - Kniazeff, Julie

PY - 2018/7/10

Y1 - 2018/7/10

N2 - G protein coupled receptors (GPCRs) play essential roles in intercellular communication. Although reported two decades ago, the assembly of GPCRs into dimer and larger oligomers in their native environment is still a matter of intense debate. Here, using number and brightness analysis of fluorescently labeled receptors in cultured hippocampal neurons, we confirm that the metabotropic glutamate receptor type 2 (mGlu2) is a homodimer at expression levels in the physiological range, while heterodimeric GABAB receptors form larger complexes. Surprisingly, we observed the formation of larger mGlu2 oligomers upon both activation and inhibition of the receptor. Stabilizing the receptor in its inactive conformation using biochemical constraints also led to the observation of oligomers. Following our recent observation that mGlu receptors are in constant and rapid equilibrium between several states under basal conditions, we propose that this structural heterogeneity limits receptor oligomerization. Such assemblies are expected to stabilize either the active or the inactive state of the receptor.

AB - G protein coupled receptors (GPCRs) play essential roles in intercellular communication. Although reported two decades ago, the assembly of GPCRs into dimer and larger oligomers in their native environment is still a matter of intense debate. Here, using number and brightness analysis of fluorescently labeled receptors in cultured hippocampal neurons, we confirm that the metabotropic glutamate receptor type 2 (mGlu2) is a homodimer at expression levels in the physiological range, while heterodimeric GABAB receptors form larger complexes. Surprisingly, we observed the formation of larger mGlu2 oligomers upon both activation and inhibition of the receptor. Stabilizing the receptor in its inactive conformation using biochemical constraints also led to the observation of oligomers. Following our recent observation that mGlu receptors are in constant and rapid equilibrium between several states under basal conditions, we propose that this structural heterogeneity limits receptor oligomerization. Such assemblies are expected to stabilize either the active or the inactive state of the receptor.

U2 - 10.1038/s41598-018-28682-6

DO - 10.1038/s41598-018-28682-6

M3 - Journal article

C2 - 29991736

VL - 8

SP - 10414

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

ER -

ID: 200178030