Abstract
We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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CHO Cells
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Calcium / metabolism
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Catalytic Domain
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Cations / metabolism
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Cell Line
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Cricetinae
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DNA, Complementary
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Electric Conductivity
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Humans
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Ion Channels / chemistry
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Ion Channels / genetics*
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Ion Channels / metabolism*
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Membrane Proteins*
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Mice
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Molecular Sequence Data
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Mutation
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Myelin Basic Protein / metabolism
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Patch-Clamp Techniques
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Phosphorylation
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Protein Kinases / chemistry
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Protein Kinases / genetics*
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Protein Kinases / metabolism*
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Protein Serine-Threonine Kinases
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Rats
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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TRPM Cation Channels
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Transfection
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Two-Hybrid System Techniques
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Type C Phospholipases / metabolism
Substances
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Cations
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DNA, Complementary
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Ion Channels
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Membrane Proteins
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Myelin Basic Protein
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Recombinant Fusion Proteins
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TRPM Cation Channels
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Adenosine Triphosphate
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Protein Kinases
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Trpm7 protein, mouse
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Protein Serine-Threonine Kinases
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TRPM7 protein, human
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Trpm7 protein, rat
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Type C Phospholipases
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Calcium