Mruk, KarenKobertz, William R.2022-08-232022-08-232009-01-212009-04-01<p>PLoS ONE. 2009;4(1):e4236. Epub 2009 Jan 21. <a href="http://dx.doi.org/10.1371/journal.pone.0004236" target="_blank">Link to article on publisher's site</a></p>1932-620310.1371/journal.pone.000423619156197https://hdl.handle.net/20.500.14038/33039KCNQ1 voltage-gated K(+) channels (Kv7.1) associate with the family of five KCNE peptides to form complexes with diverse gating properties and pharmacological sensitivities. The varied gating properties of the different KCNQ1-KCNE complexes enables the same K(+) channel to function in both excitable and non excitable tissues. Small molecule activators would be valuable tools for dissecting the gating mechanisms of KCNQ1-KCNE complexes; however, there are very few known activators of KCNQ1 channels and most are ineffective on the physiologically relevant KCNQ1-KCNE complexes. Here we show that a simple boronic acid, phenylboronic acid (PBA), activates KCNQ1/KCNE1 complexes co-expressed in Xenopus oocytes at millimolar concentrations. PBA shifts the voltage sensitivity of KCNQ1 channel complexes to favor the open state at negative potentials. Analysis of different-sized charge carriers revealed that PBA also targets the permeation pathway of KCNQ1 channels. Activation by the boronic acid moiety has some specificity for the Kv7 family members (KCNQ1, KCNQ2/3, and KCNQ4) since PBA does not activate Shaker or hERG channels. Furthermore, the commercial availability of numerous PBA derivatives provides a large class of compounds to investigate the gating mechanisms of KCNQ1-KCNE complexes.en-USBiochemistry, Biophysics, and Structural BiologyJournal Articlehttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=2588&amp;context=gsbs_sp&amp;unstamped=1https://escholarship.umassmed.edu/gsbs_sp/1589807880gsbs_sp/1589