Reciprocal Regulation in Phosphotyrosine
and Potassium Channel Signaling

Voltage-gated potassium (Kv) channels are phosphorylated and modulated by endogenous and expressed protein tyrosine kinases. In turn, protein tyrosine phosphorylation by endogenous and expressed tyrosine kinases is reduced markedly by the expression of functional Kv channels. The levels of tyrosine kinase protein and cellular protein substrates are unaffected, consistent with a reduction in tyrosine phosphorylation that results from inhibition of protein tyrosine kinase activity. The attenuation of protein tyrosine phosphorylation is correlated with the gating properties of expressed wild type and mutant Kv channels. Furthermore, protein tyrosine phosphorylation is reduced within minutes by acute treatment with the electrogenic potassium ionophore valinomycin. Because tyrosine phosphorylation is known to influence Kv channel activity, these results suggest that reciprocal modulatory interactions occur between Kv channel and tyrosine phosphorylation signaling pathways.

Speaker Schedule  |  Reports from Previous Years
Top of Page | Life Sciences | Brandeis University