GΒ5 recruits R7 RGS proteins to GIRK channels to regulate the timing of neuronal inhibitory signaling

K. Xie; K.L. Allen; S. Kourrich; J. Colón-Saez; M.J. Thomas; K. Wickman; K.A. Martemyanov

doi:10.1038/nn.2549

Back

Journal article

GΒ5 recruits R7 RGS proteins to GIRK channels to regulate the timing of neuronal inhibitory signaling

K. Xie, K.L. Allen, S. Kourrich, J. Colón-Saez, M.J. Thomas, K. Wickman and K.A. Martemyanov

Nature Neuroscience, Vol.13(6), pp.661-663

2010

DOI: https://doi.org/10.1038/nn.2549

PMID: 20453851

Abstract

Animals

Baclofen

Cell Line

Cells, Cultured

G Protein-Coupled Inwardly-Rectifying Potassium Channels

GABA Agonists

GTP-Binding Protein beta Subunits

Hippocampus

Humans

Inhibitory Postsynaptic Potentials

Membrane Potentials

Mice

Mice, Inbred C57BL

Mice, Knockout

Motor Activity

Neural Inhibition

Neurons

Receptors, GABA-B

RGS Proteins

Synaptic Transmission

Time Factors

baclofen

G protein coupled inwardly rectifying potassium channel

guanine nucleotide binding protein beta subunit

neurotransmitter

phosphatidylinositol 3 kinase gamma

phospholipase C beta2

potassium channel

RGS protein

RGS7 protein

RGS9 protein

unclassified drug

4 aminobutyric acid B receptor

4 aminobutyric acid receptor stimulating agent

baclofen

G protein coupled inwardly rectifying potassium channel

Gnb5 protein, mouse

guanine nucleotide binding protein beta subunit

RGS protein

Rgs7 protein, mouse

article

cell compartmentalization

controlled study

genetic transfection

hippocampus

human

human cell

immunoblotting

immunoprecipitation

kinetics

locomotion

nerve cell inhibition

postsynaptic inhibition

priority journal

signal transduction

animal

C57BL mouse

cell culture

cell line

cell membrane potential

drug effect

genetics

inhibitory postsynaptic potential

metabolism

motor activity

mouse

mouse mutant

nerve cell

physiology

synaptic transmission

time

The type 5 G protein Β subunit (GΒ5) can form complexes with members of the regulator of G protein signaling 7 (RGS7) family, but its relevance to neuronal G protein signaling is unclear. We found that mouse RGS7-GΒ5 complexes bound to G protein-gated potassium channels and facilitated their functional coupling to GABA B receptors in neurons. Our findings identify a compartmentalization mechanism that is critical for ensuring high temporal resolution of neuronal G protein signaling. © 2010 Nature America, Inc. All rights reserved.

Files and links (1)

url

https://www.scopus.com/inward/record.uri?eid=2-s2.0-77952886365&doi=10.1038%2fnn.2549&partnerID=40&md5=befd9e475ea251c44398bc5c4b74e2e6View

Metrics

2 Record Views

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Citation topics: 1 Clinical & Life Sciences; 1.159 Membrane Channels & Receptors; 1.159.426 GPCR Signaling
Web Of Science research areas: Neurosciences
ESI research areas: Neuroscience & Behavior

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

Source: InCites

Details

Title: GΒ5 recruits R7 RGS proteins to GIRK channels to regulate the timing of neuronal inhibitory signaling
Creators: K. Xie - University of Minnesota
K.L. Allen - University of Minnesota
S. Kourrich - University of Minnesota
J. Colón-Saez - University of Minnesota
M.J. Thomas - University of Minnesota
K. Wickman - University of Minnesota
K.A. Martemyanov - Twin Cities Orthopedics
Publication Details: Nature Neuroscience, Vol.13(6), pp.661-663
Grant note: US National Institutes of Health: DA021743, DA026405, EY018139, MH061933, DA011806, DA019666, MII078291 McKnight Land-Grant AwardWhitehall Foundation
We thank J. Chen for providing the G beta 5^-/- mice, W. Simonds for the gift of antibodies to G beta 5 and RGS7 and M. Parent for assistance with the hippocampal slicing technique. This work was supported by US National Institutes of Health grants DA021743 (K.A.M.), DA026405 (K.A.M.), EY018139 (K.A.M.), MH061933 (K.W.), DA011806 (K.W.), DA019666 (M.J.T.) and MII078291 (J.C.- S.), a McKnight Land-Grant Award (K.A.M), and an award from the Whitehall Foundation (M.J.T.).
Comment: Export Date: 24 October 2025; Cited By: 63; CODEN: NANEF
Academic Unit: Physiology and Biophysics Research; Miller School of Medicine
Resource Type: Journal article
PMID: 20453851
Record Identifier: 991032828751602976