The K+ channel inward rectifier subunits form a channel similar to neuronal G protein-gated K+ channel
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چکیده
منابع مشابه
Conversion of a Delayed Rectifier K+ Channel to a Voltage-Gated Inward Rectifier K+ Channel by Three Amino Acid Substitutions
Single, double, and triple mutations progressively shift Shaker activation to more hyperpolarized potentials, resulting in an increase in the fraction of inactivated channels at negative resting voltages. The most negatively shifted mutation, the triple mutant, behaves like an inward rectifier. What is usually considered activation of an inward rectifier is, for the triple mutant, recovery from...
متن کاملAnchoring proteins confer G protein sensitivity to an inward-rectifier K(+) channel through the GK domain.
Anchoring proteins cluster receptors and ion channels at postsynaptic membranes in the brain. They also act as scaffolds for intracellular signaling molecules including synGAP and NO synthase. Here we report a new function for intracellular anchoring proteins: the regulation of synaptic ion channel function. A neuronal G protein-gated inwardly rectifying K(+) channel, Kir3.2c, can not be activa...
متن کاملIntrinsic gating properties of a cloned G protein-activated inward rectifier K+ channel
The voltage-, time-, and K(+)-dependent properties of a G protein-activated inwardly rectifying K+ channel (GIRK1/KGA/Kir3.1) cloned from rat atrium were studied in Xenopus oocytes under two-electrode voltage clamp. During maintained G protein activation and in the presence of high external K+ (VK = 0 mV), voltage jumps from VK to negative membrane potentials activated inward GIRK1 K+ currents ...
متن کاملA Novel Inward Rectifier K+ Channel with Unique Pore Properties
We have cloned a novel K+-selective, inward rectifier channel that is widely expressed in brain but is especially abundant in the Purkinje cell layer of the cerebellum and pyramidal cells of the hippocampus. It is also present in a wide array of tissues, including kidney and intestine. The channel is only 38% identical to its closest relative, Kir1.3 (Kir1-ATP-regulated inward rectifier K+ [ROM...
متن کاملSubunit stoichiometry of a heteromultimeric G protein-coupled inward-rectifier K+ channel.
We investigated the stoichiometry of the heteromultimeric G protein-coupled inward-recitfier K+ channel (GIRK) formed from GIRK1 and GIRK4 subunits. Multimeric GIRK constructs with several concatenated channel subunits were expressed in Xenopus oocytes. Coexpression of various trimeric constructs with different monomers clearly showed that the functional channel has stoichiometry (GIRK1)2(GIRK4...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1996
ISSN: 0014-5793
DOI: 10.1016/0014-5793(95)01465-9