Abstract
Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSlo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSlo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila EAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat Kv1.3. Confocal fluorescence microscopy demonstrates that Slob and dSlo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSlo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel-binding proteins.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibody Specificity
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Calcium / physiology*
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Cells, Cultured
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Chromosome Mapping
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Drosophila / genetics*
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Drosophila Proteins*
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Electrophysiology
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Humans
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Kidney / cytology
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Large-Conductance Calcium-Activated Potassium Channel alpha Subunits
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Large-Conductance Calcium-Activated Potassium Channels
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Molecular Sequence Data
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Potassium Channels / genetics*
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Potassium Channels / immunology
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Potassium Channels / metabolism*
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Potassium Channels, Calcium-Activated*
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Precipitin Tests
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Protein Binding / physiology
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Rabbits
Substances
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Drosophila Proteins
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KCNMA1 protein, human
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Large-Conductance Calcium-Activated Potassium Channel alpha Subunits
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Large-Conductance Calcium-Activated Potassium Channels
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Potassium Channels
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Potassium Channels, Calcium-Activated
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Slob protein, Drosophila
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slo protein, Drosophila
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Calcium