Assignment of Human G-Protein-Coupled Inward Rectifier K+Channel Homolog GIRK3 Gene to Chromosome 1q21–q23

Genomics ◽  
1995 ◽  
Vol 29 (3) ◽  
pp. 808-809 ◽  
Author(s):  
F. Lesage ◽  
M. Fink ◽  
J. Barhanin ◽  
M. Lazdunski ◽  
M.-G. Mattéi
Keyword(s):  
G Protein ◽  
Inward Rectifier ◽  
K Channel ◽  
G Protein Coupled ◽  
Chromosome 1Q21

scholarly journals Subunit Stoichiometry of a Heteromultimeric G protein-coupled Inward-rectifier K+Channel

1996 ◽  
Vol 271 (48) ◽  
pp. 30524-30528 ◽  
Author(s):  
Scott K. Silverman ◽  
Henry A. Lester ◽  
Dennis A. Dougherty
Keyword(s):  
G Protein ◽  
Inward Rectifier ◽  
K Channel ◽  
Subunit Stoichiometry ◽  
G Protein Coupled

scholarly journals Primary structure and functional expression of a mouse inward rectifier K+ channel and rat G-protein-coupled muscarinic K+ channel.

1995 ◽  
Vol 15 (2) ◽  
pp. 106-113
Author(s):  
Yoshihiro Kubo ◽  
Eitan Reuveny ◽  
Paul A Slesinger ◽  
Timothy J Baldwin ◽  
Yuh Nung Jan ◽  
...  
Keyword(s):  
G Protein ◽  
Primary Structure ◽  
Functional Expression ◽  
Inward Rectifier ◽  
K Channel ◽  
G Protein Coupled

scholarly journals Interaction Sites of the G Protein β Subunit with Brain G Protein-coupled Inward Rectifier K+Channel

2001 ◽  
Vol 276 (16) ◽  
pp. 12712-12717 ◽  
Author(s):  
Abla M. Albsoul-Younes ◽  
Pamela M. Sternweis ◽  
Peng Zhao ◽  
Hiroko Nakata ◽  
Shigehiro Nakajima ◽  
...  
Keyword(s):  
G Protein ◽  
Inward Rectifier ◽  
K Channel ◽  
Β Subunit ◽  
Interaction Sites ◽  
G Protein Coupled

Single-channel properties of a G-protein-coupled inward rectifier potassium channel in brain neurons

1996 ◽  
Vol 75 (1) ◽  
pp. 318-328 ◽  
Author(s):  
J. J. Grigg ◽  
T. Kozasa ◽  
Y. Nakajima ◽  
S. Nakajima
Keyword(s):  
G Protein ◽  
Single Channel ◽  
Inward Rectifier ◽  
Equilibrium Potential ◽  
K Channel ◽  
Open Probability ◽  
K Concentration ◽  
Inwardly Rectifying ◽  
G Protein Coupled ◽  
Cytoplasmic Side

1. In cultured rat locus coeruleus neurons, somatostatin or met-enkephalin induces an inwardly rectifying K+ conductance. This inward rectifier was analyzed at the single-channel level. 2. Using the inside-out patch-clamp, guanosine 5'-triphosphate (GTP) application to the cytoplasmic side in the presence of somatostatin or met-enkephalin in the pipette produced a large increase in channel activity, which disappeared on switching from GTP to guanosine 5'-diphosphate. 3. The unitary conductance was approximately 30 pS at -95 mV with an extracellular K+ concentration of 156 mM and an intracellular K+ concentration of 124 mM at 23 degrees C. The channel showed burst behavior, and the closed time histogram was fit by two exponentials, with the fast time constant being 0.4 ms. The burst time histogram was also fit by two exponentials, with time constants of 0.24 and 2.0 ms (at 10 nM somatostatin). When the somatostatin concentration was changed from 500 to 1 nM, the kinetic behavior of the channel did not change, except that the open probability of the patch was decreased. 4. The current-voltage relation of the unitary channel current showed inward rectification. The reversal potential coincided with the K+ equilibrium potential, and it shifted according to a change in the K+ equilibrium potential. 5. In the presence of external somatostatin, the application of guanosine 5'-O-(3-thiotriphosphate) to the cytoplasmic side induced an irreversible activation of this channel. 6. These results indicate that this K+ channel is the microscopic counterpart of the somatostatin- or met-enkephalin-induced inwardly rectifying K+ current in whole cell recording, and that the channel is activated by a G protein without a diffusible second messenger. Thus this channel is identified as a neuronal G-protein-coupled inward rectifier K+ channel. 7. Analysis of the burst behavior, based on a close-close-open kinetic model, revealed that there are at least four states in the K+ channel, a short gap, a longer closing, a short opening, and a long opening, and that the neuronal inward rectifier is activated at faster rates than the atrial inward rectifier.

scholarly journals Dominant negative effects of a Gβ mutant on G-protein coupled inward rectifier K+channel

FEBS Letters ◽  
2006 ◽  
Vol 580 (16) ◽  
pp. 3879-3882 ◽  
Author(s):  
Qi Zhao ◽  
Abla M. Albsoul-Younes ◽  
Peng Zhao ◽  
Tohru Kozasa ◽  
Yasuko Nakajima ◽  
...  
Keyword(s):  
G Protein ◽  
Inward Rectifier ◽  
Dominant Negative ◽  
K Channel ◽  
Negative Effects ◽  
G Protein Coupled

scholarly journals WIN55,212-2, a Dual Modulator of Cannabinoid Receptors and G Protein-Coupled Inward Rectifier Potassium Channels

Biomedicines ◽  
2021 ◽  
Vol 9 (5) ◽  
pp. 484
Author(s):  
Dongchen An ◽  
Steve Peigneur ◽  
Jan Tytgat
Keyword(s):  
Potassium Channels ◽  
Potassium Channel ◽  
G Protein ◽  
Cannabinoid Receptors ◽  
Inward Rectifier ◽  
Xenopus Laevis Oocyte ◽  
Inward Rectifier Potassium Channels ◽  
Wide Range ◽  
Cb2 Receptors ◽  
G Protein Coupled

The coupling of cannabinoid receptors, CB1 and CB2, to G protein-coupled inward rectifier potassium channels, GIRK1 and GIRK2, modulates neuronal excitability in the human brain. The present study established and validated the functional expression in a Xenopus laevis oocyte expression system of CB1 and CB2 receptors, interacting with heteromeric GIRK1/2 channels and a regulator of G protein signaling, RGS4. This ex vivo system enables the discovery of a wide range of ligands interacting orthosterically or allosterically with CB1 and/or CB2 receptors. WIN55,212-2, a non-selective agonist of CB1 and CB2, was used to explore the CB1- or CB2-GIRK1/2-RGS4 signaling cascade. We show that WIN55,212-2 activates CB1 and CB2 at low concentrations whereas at higher concentrations it exerts a direct block of GIRK1/2. This illustrates a dual modulatory function, a feature not described before, which helps to explain the adverse effects induced by WIN55,212-2 in vivo. When comparing the effects with other typical cannabinoids such as Δ9-THC, CBD, CP55,940, and rimonabant, only WIN55,212-2 can significantly block GIRK1/2. Interestingly, the inward rectifier potassium channel, IRK1, a non-G protein-coupled potassium channel important for setting the resting membrane voltage and highly similar to GIRK1 and GIRK2, is not sensitive to WIN55,212-2, Δ9-THC, CBD, CP55,940, or rimonabant. From this, it is concluded that WIN55,212-2 selectively blocks GIRK1/2.

scholarly journals Modulation of human erg K+channel gating by activation of a G protein-coupled receptor and protein kinase C

1998 ◽  
Vol 511 (2) ◽  
pp. 333-346 ◽  
Author(s):  
Francisco Barros ◽  
David Gómez-Varela ◽  
Cristina G. Viloria ◽  
Teresa Palomero ◽  
Teresa Giráldez ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
G Protein ◽  
Channel Gating ◽  
K Channel ◽  
G Protein Coupled Receptor ◽  
Kinase C ◽  
G Protein Coupled
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