Holmes T C, Berman K, Swartz J E, Dagan D, Levitan I B
Department of Biochemistry and Volen Center for Complex Systems, Brandeis University, Waltham, Massachusetts 02254, USA.
J Neurosci. 1997 Dec 1;17(23):8964-74. doi: 10.1523/JNEUROSCI.17-23-08964.1997.
Protein tyrosine phosphorylation by endogenous and expressed tyrosine kinases is reduced markedly by the expression of functional voltage-gated potassium (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, cellular protein tyrosine phosphorylation is reduced within minutes by acute treatment with the electrogenic potassium ionophore valinomycin. Because tyrosine phosphorylation in turn influences Kv channel activity, these results suggest that reciprocal modulatory interactions occur between Kv channel and protein tyrosine phosphorylation signaling pathways.
功能性电压门控钾（Kv）通道的表达可显著降低内源性和表达型酪氨酸激酶引起的蛋白质酪氨酸磷酸化。酪氨酸激酶蛋白和细胞蛋白底物的水平未受影响，这与蛋白质酪氨酸激酶活性受抑制导致的酪氨酸磷酸化减少相一致。蛋白质酪氨酸磷酸化的减弱与所表达的野生型和突变型Kv通道的门控特性相关。此外，用生电钾离子载体缬氨霉素进行急性处理可在数分钟内降低细胞蛋白酪氨酸磷酸化。由于酪氨酸磷酸化反过来会影响Kv通道活性，这些结果表明Kv通道与蛋白质酪氨酸磷酸化信号通路之间存在相互调节的相互作用。
