Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel
about
PIP3 inhibition of RGS protein and its reversal by Ca2+/calmodulin mediate voltage-dependent control of the G protein cycle in a cardiac K+ channel.Graded contribution of the Gbeta gamma binding domains to GIRK channel activation.Regulators of G-protein signaling form a quaternary complex with the agonist, receptor, and G-protein. A novel explanation for the acceleration of signaling activation kinetics.Agonist unbinding from receptor dictates the nature of deactivation kinetics of G protein-gated K+ channelsCell signal control of the G protein-gated potassium channel and its subcellular localization.How regulators of G protein signaling achieve selective regulation.The Possible Role of TASK Channels in Rank-Ordered Recruitment of Motoneurons in the Dorsolateral Part of the Trigeminal Motor Nucleus.RGS4 regulates partial agonism of the M2 muscarinic receptor-activated K+ currents.Gating properties of GIRK channels activated by Galpha(o)- and Galpha(i)-coupled muscarinic m2 receptors in Xenopus oocytes: the role of receptor precoupling in RGS modulation.Structural determinants at the M2 muscarinic receptor modulate the RGS4-GIRK response to pilocarpine by impairment of the receptor voltage sensitivity.RGS Proteins in Heart: Brakes on the Vagus.Short-term desensitization of muscarinic K+ current in the heart.Phosphatidylinositol 3,4,5-trisphosphate and Ca2+/calmodulin competitively bind to the regulators of G-protein-signalling (RGS) domain of RGS4 and reciprocally regulate its actionCellular modelling: experiments and simulation to develop a physiological model of G-protein control of muscarinic K+ channels in mammalian atrial cells.RGS3 and RGS4 differentially associate with G protein-coupled receptor-Kir3 channel signaling complexes revealing two modes of RGS modulation. Precoupling and collision coupling.RGS proteins maintain robustness of GPCR-GIRK coupling by selective stimulation of the G protein subunit Gαo.
P2860
Q34047720-07730E2E-D00C-4BE5-BF57-9DCC01A45391Q34075992-B3EDB88D-2547-4DA7-93F9-EA109912C249Q34389034-FAE787B0-C1DC-400B-80EA-339A2093159AQ35023353-DC491971-0308-4B39-BCDC-065B9E07298BQ35201276-9CA65679-62F4-495B-9FEE-72D6A08EC8F3Q35652043-C4500041-4061-452F-9799-F58536217919Q37110555-5EB17688-8ED3-4BFA-98B7-8EEEB75FEBCEQ37652030-0A29CB04-7461-4915-AE98-D82844BCAFEAQ38360388-09A314E2-45FE-41EE-B9BB-5B1D90D0FEE7Q41094207-39BFAFF8-4E28-4252-8512-9B7E9F6AB895Q41875965-1BCC429D-6360-4E3B-957E-DCC48C7A8C51Q42094627-C24D6CB6-3F96-418C-8FEC-D6BFBC7A531BQ42156610-D3633B3A-5D06-4687-AA2B-BA44D2FE51B7Q43061155-F6B2615E-9A89-45D3-81E6-D8B23A7F28ACQ48420912-F2C85746-B421-49F4-B901-3C6EC28F44BCQ48655186-A9694AF6-7F43-468A-B155-84778A11FB53
P2860
Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Interaction between the RGS do ...... rotein-gated potassium channel
@ast
Interaction between the RGS do ...... rotein-gated potassium channel
@en
Interaction between the RGS do ...... rotein-gated potassium channel
@nl
type
label
Interaction between the RGS do ...... rotein-gated potassium channel
@ast
Interaction between the RGS do ...... rotein-gated potassium channel
@en
Interaction between the RGS do ...... rotein-gated potassium channel
@nl
prefLabel
Interaction between the RGS do ...... rotein-gated potassium channel
@ast
Interaction between the RGS do ...... rotein-gated potassium channel
@en
Interaction between the RGS do ...... rotein-gated potassium channel
@nl
P2093
P2860
P3181
P1476
Interaction between the RGS do ...... rotein-gated potassium channel
@en
P2093
K Matsushita
P2860
P304
P3181
P356
10.1111/J.1469-7793.2001.T01-1-00133.X
P407
P577
2001-08-15T00:00:00Z