Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel (Q28346089)

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Language	Label	Description	Also known as
English	Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel	scientific article

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scholarly article

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Interaction between the RGS domain of RGS4 with G protein alpha subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel (English)

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author name string

A Inanobe

1

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S Fujita

2

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Y Makino

3

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K Matsushita

4

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M Ishii

5

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M Chachin

6

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Y Kurachi

7

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language of work or name

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publication date

15 August 2001

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Journal of Physiology

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535

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Pt 1

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133-43

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G protein regulation of potassium ion channels

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Divergence of RGS proteins: evidence for the existence of six mammalian RGS subfamilies

1 reference

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Emerging roles for RGS proteins in cell signalling

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New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes

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Evidence that the nucleotide exchange and hydrolysis cycle of G proteins causes acute desensitization of G-protein gated inward rectifier K+ channels

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Residues and mechanisms for slow activation and Ba2+ block of the cardiac muscarinic K+ channel, Kir3.1/Kir3.4.

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Molecular properties of neuronal G-protein-activated inwardly rectifying K+ channels.

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Relaxation of the ACh-induced potassium current in the rabbit sinoatrial node cell

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RGS4 binds to membranes through an amphipathic alpha -helix.

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A regulator of G protein signalling (RGS) protein confers agonist-dependent relaxation gating to a G protein-gated K+ channel

1 reference

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Cloning of a Xenopus laevis inwardly rectifying K+ channel subunit that permits GIRK1 expression of IKACh currents in oocytes

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Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel

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Mutational analysis of the Asn residue essential for RGS protein binding to G-proteins

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The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling

1 reference

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