Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit

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

Standard

Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. / Tsai, Ching-Ju; Marino, Jacopo; Adaixo, Ricardo; Pamula, Filip; Muehle, Jonas; Maeda, Shoji; Flock, Tilman; Taylor, Nicholas MI; Mohammed, Inayatulla; Matile, Hugues; Dawson, Roger Jp; Deupi, Xavier; Stahlberg, Henning; Schertler, Gebhard.

In: eLife, Vol. 8, e46041, 2019.

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

Harvard

Tsai, C-J, Marino, J, Adaixo, R, Pamula, F, Muehle, J, Maeda, S, Flock, T, Taylor, NMI, Mohammed, I, Matile, H, Dawson, RJ, Deupi, X, Stahlberg, H & Schertler, G 2019, 'Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit', eLife, vol. 8, e46041. https://doi.org/10.7554/eLife.46041

APA

Tsai, C-J., Marino, J., Adaixo, R., Pamula, F., Muehle, J., Maeda, S., Flock, T., Taylor, N. MI., Mohammed, I., Matile, H., Dawson, R. J., Deupi, X., Stahlberg, H., & Schertler, G. (2019). Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. eLife, 8, [e46041]. https://doi.org/10.7554/eLife.46041

Vancouver

Tsai C-J, Marino J, Adaixo R, Pamula F, Muehle J, Maeda S et al. Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. eLife. 2019;8. e46041. https://doi.org/10.7554/eLife.46041

Author

Tsai, Ching-Ju ; Marino, Jacopo ; Adaixo, Ricardo ; Pamula, Filip ; Muehle, Jonas ; Maeda, Shoji ; Flock, Tilman ; Taylor, Nicholas MI ; Mohammed, Inayatulla ; Matile, Hugues ; Dawson, Roger Jp ; Deupi, Xavier ; Stahlberg, Henning ; Schertler, Gebhard. / Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. In: eLife. 2019 ; Vol. 8.

Bibtex

@article{8f90f5e0768e472d8972b99f7ff58b5f,
title = "Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit",
abstract = "One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway.",
author = "Ching-Ju Tsai and Jacopo Marino and Ricardo Adaixo and Filip Pamula and Jonas Muehle and Shoji Maeda and Tilman Flock and Taylor, {Nicholas MI} and Inayatulla Mohammed and Hugues Matile and Dawson, {Roger Jp} and Xavier Deupi and Henning Stahlberg and Gebhard Schertler",
year = "2019",
doi = "10.7554/eLife.46041",
language = "English",
volume = "8",
journal = "eLife",
issn = "2050-084X",
publisher = "eLife Sciences Publications Ltd.",

}

RIS

TY - JOUR

T1 - Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit

AU - Tsai, Ching-Ju

AU - Marino, Jacopo

AU - Adaixo, Ricardo

AU - Pamula, Filip

AU - Muehle, Jonas

AU - Maeda, Shoji

AU - Flock, Tilman

AU - Taylor, Nicholas MI

AU - Mohammed, Inayatulla

AU - Matile, Hugues

AU - Dawson, Roger Jp

AU - Deupi, Xavier

AU - Stahlberg, Henning

AU - Schertler, Gebhard

PY - 2019

Y1 - 2019

N2 - One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway.

AB - One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway.

U2 - 10.7554/eLife.46041

DO - 10.7554/eLife.46041

M3 - Journal article

C2 - 31251171

VL - 8

JO - eLife

JF - eLife

SN - 2050-084X

M1 - e46041

ER -

ID: 227087713