Abstract
KCNE1 is known to modulate the voltage-gated potassium channel ? subunit KCNQ1 to generate slowly activating potassium currents. This potassium channel is essential for the cardiac action potential that mediates a heartbeat as well as the potassium ion homeostasis in the inner ear. Therefore it is important to know the structure and dynamics of KCNE1 to better understand its modulatory role. Previously the Sanders group solved the three-dimensional structure of KCNE1 in LMPG micelles, which yielded a better understanding of this KCNQ1/KCNE1 channel activity. However, research in the Lorigan group showed different structural properties of KCNE1 when incorporated into POPC/POPG lipid bilayers as opposed to LMPG micelles. It is hence necessary to study the structure of KCNE1 in a more native-like environment such as multi-lamellar vesicles (MLVs). In this study, the dynamics of lipid bilayers upon incorporation of the membrane protein KCNE1 were investigated using (31) P solid-state NMR spectroscopy. Specifically, the protein/lipid interaction was studied at varying molar ratios of protein to lipid content. The static (31) P NMR and T1 relaxation time were investigated. The (31) P NMR powder spectra indicated significant perturbations of KCNE1 on the phospholipid headgroups of MLVs as shown from the changes in the (31) P spectral line shape and the chemical shift anisotropy (CSA) line width. (31) P T1 relaxation times were shown to be reversely proportional to the molar ratios of KCNE1 incorporated. The (31) P NMR data clearly indicate that KCNE1 interacts with the membrane.
PMID: 28233402 [PubMed - as supplied by publisher]
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Linear Mode
