Regulation of wild-type and mutant KCNQ1/KCNE1 channels by tyrosine kinase.

Pflügers Archiv : European journal of physiology
Sergey MissanPaul Linsdell

Abstract

The objective of the study was to investigate the role of tyrosine phosphorylation in the regulation of KCNQ1/KCNE1 channels. Large whole-cell time- and voltage-dependent K(+) currents were present in human embryonic kidney 293 cells cotransfected with human KCNQ1 and KCNE1 but not in control nontransfected cells. The time- and voltage-dependent current had biophysical properties typical of cardiac KCNQ1/KCNE1 current and was almost completely abolished by KCNQ1 blocker chromanol 293B (50 microM). Both KCNQ1/KCNE1 and KCNQ1 current were inhibited in a voltage-independent manner by tyrosine kinase (PTK) inhibitor tyrphostin A25 (100 microM), but not by PTK-inactive tyrphostin A1 (100 microM), suggesting involvement of tyrosine phosphorylation in maintaining channel activity. This view was strengthened by the finding that phosphotyrosyl phosphatase inhibitor monoperoxo(picolinato)-oxo-vanadate(V) (200 microM) reversed the inhibition of current by tyrphostin A25. However, the channel-pertinent tyrosine phosphorylation modulated by these compounds does not appear to be on the channel itself because inhibition of current by tyrphostin A25 was unaffected by single and multiple mutations of KCNQ1 cytoplasmically accessible tyrosine re...Continue Reading

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Citations

Jul 20, 2011·Clinica Chimica Acta; International Journal of Clinical Chemistry·Chia-Ti TsaiJuey-Jen Hwang
Nov 9, 2011·Biochimica Et Biophysica Acta·Wei WuGui-Rong Li
Jan 21, 2010·Biochimica Et Biophysica Acta·Ming-Qing DongGui-Rong Li
Apr 22, 2011·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Minna HassinenMatti Vornanen
Aug 8, 2020·Cells·Irene EstadellaAntonio Felipe

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