Science · 2001 · 733 citations · 9 references
Life SciencesBiochemistryMolecular BiologyElectrophysiologyIon Channel BiophysicsSignal TransductionCalcium SignalingIon Channel ExpressionIon Channel PhysiologyIon Channel RegulationIon Channel SignalingIon ChannelsCell Division ControlIon Channel FunctionIon Channel PhosphorylationIon Channel SelectivityTransient Receptor Potential Channel FunctionZinc Finger DomainsZinc Finger MotifsZinc Finger Proteins
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.
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