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J Biol Chem, Vol. 273, Issue 51, 34063-34068, December 18, 1998
From the Department of Molecular Neurobiology of Signal
Transduction, Max-Planck-Institute for Biophysical Chemistry, 37070 Göttingen, Germany
Signaling via cytosolic and receptor tyrosine
kinases is associated with cell growth and differentiation but also
targets onto transmitter receptors and ion channels. Here, regulation by tyrosine kinase (TK) activity was investigated for inwardly rectifying K+ (Kir2.1) channels that control membrane
excitability in many central neurons. In mammalian tsA-201 cells, the
membrane-permeable protein tyrosine phosphatase inhibitor,
perorthovanadate (100 µM), suppressed currents through
recombinant Kir2.1 channels by 60 ± 20%. Coapplication of the TK
inhibitor genistein (100 µM) completely abolished this
effect. Native Kir2.1 channels in rat basophilic leukocytes were
affected by manipulation of the TK and protein tyrosine phosphatase
activity in a qualitatively similar manner. Site mutation of a tyrosine
consensus residue for TK phosphorylation in the C-terminal domain of
Kir2.1 generated channel properties indistinguishable from wild-type
Kir2.1 channels. However, Kir2.1Y242F channels were no longer
suppressed following exposure to perorthovanadate, indicating that the
channel is a direct substrate for TKs. After coexpression of nerve
growth factor receptor with Kir2.1 channels in tsA-201 cells and
Xenopus oocytes, the activity of Kir2.1 was rapidly
suppressed by applied nerve growth factor (0.5 µg/ml) by 31 ± 10 and 21 ± 15%, respectively. Acute inhibition was also evoked
by epidermal growth factor and insulin via endogenous insulin receptors, indicating that Kir2.1 channels may serve as a general target for neurotrophic growth factors in the brain.
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