Abstract
Cerebellar granule neurons possess a non-inactivating K+ current, which controls resting membrane potentials and modulates the firing rate by means of muscarinic agonists. kcr1 was cloned from the cerebellar cDNA library by suppression cloning. KCR1 is a novel protein with 12 putative transmembrane domains and enhances the functional expression of the cerebellar non-inactivating K+ current in Xenopus oocytes. KCR1 also accelerates the activation of rat EAG K+ channels expressed in Xenopus oocytes or in COS-7 cells. Far-Western blotting revealed that KCR1 and EAG proteins interacted with each other by means of their C-terminal regions. These results suggest that KCR1 is the regulatory component of non-inactivating K+ channels.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cerebellum / physiology*
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Cloning, Molecular
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DNA, Antisense / pharmacology
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DNA, Complementary / genetics
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Electric Conductivity
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Ether-A-Go-Go Potassium Channels
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Ion Channel Gating / drug effects
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Magnesium / pharmacology
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Membrane Potentials / physiology*
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Models, Molecular
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Molecular Sequence Data
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism*
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Potassium / metabolism*
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Potassium Channels / genetics
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Potassium Channels / metabolism*
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Protein Binding
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Protein Biosynthesis
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RNA, Messenger / genetics
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Rats
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Recombinant Proteins / metabolism
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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Xenopus
Substances
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Alg10 protein, rat
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DNA, Antisense
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DNA, Complementary
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Ether-A-Go-Go Potassium Channels
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Nerve Tissue Proteins
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Potassium Channels
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RNA, Messenger
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Recombinant Proteins
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Magnesium
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Potassium
Associated data
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GENBANK/U78090
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GENBANK/Z69728
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GENBANK/Z81131