Determination of the Stoichiometry between α- and γ1 Subunits of the BK Channel Using LRET.
Ontology highlight
ABSTRACT: Two families of accessory proteins, β and γ, modulate BK channel gating and pharmacology. Notably, in the absence of internal Ca2+, the γ1 subunit promotes a large shift of the BK conductance-voltage curve to more negative potentials. However, very little is known about how α- and γ1 subunits interact. In particular, the association stoichiometry between both subunits is unknown. Here, we propose a method to answer this question using lanthanide resonance energy transfer. The method assumes that the kinetics of lanthanide resonance energy transfer-sensitized emission of the donor double-labeled α/γ1 complex is the linear combination of the kinetics of the sensitized emission in single-labeled complexes. We used a lanthanide binding tag engineered either into the α- or the γ1 sub
SUBMITTER: Carrasquel-Ursulaez W
PROVIDER: S-EPMC6129150 | biostudies-literature | 2018 Jun
REPOSITORIES: biostudies-literature
ACCESS DATA