Photo-Cross-Linking of I_Ks Demonstrates State-Dependent Interactions between KCNE1 and KCNQ1.

ABSTRACT: The slow delayed rectifier potassium current (I_Ks) is a key repolarizing current during the cardiac action potential. It consists of four KCNQ1 α-subunits and up to four KCNE1 β-subunits, which are thought to reside within external clefts of the channel. The interaction of KCNE1 with KCNQ1 dramatically delays opening of the channel but the mechanisms by which this occur are not yet fully understood. Here, we have used unnatural amino acid photo-cross-linking to investigate the dynamic interactions that occur between KCNQ1 and KCNE1 during activation gating. The unnatural amino acid p-Benzoylphenylalanine was successfully incorporated into two residues within the transmembrane domain of KCNE1: F56 and F57. UV-induced cross-linking suggested that F56Bpa interacts with KCNQ1 in the

SUBMITTER: Westhoff M 

PROVIDER: S-EPMC5529200 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature