Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity.

ABSTRACT: Gating of the outward-rectifying K+ channel TOK1 of Saccharomyces cerevisiae is controlled by membrane voltage and extracellular K+ concentration. Previous studies identified two kinetically distinct effects of K+, and site-mutagenic analysis associated these K+-dependencies with domains of the extracellular turrets of the channel protein. We have mapped the TOK1 pore domains to extant K+ channel crystal structures to target additional residues contributing to TOK1 gating. Leu270, located in the first pore domain of TOK1, was found to be critical for gating and its K+ sensitivity. Analysis of amino acid substitutions indicated that spatial position of the polypeptide backbone is a primary factor determining gating sensitivity to K+. The strongest effects, with L270Y, L270F and L270W, led t

SUBMITTER: Johansson I 

PROVIDER: S-EPMC1360717 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature