Lipid-Protein Interactions in the Regulated Betaine Symporter BetP Probed by Infrared Spectroscopy.

ABSTRACT: The Na(+)-coupled betaine symporter BetP senses changes in the membrane state and increasing levels of cytoplasmic K(+) during hyperosmotic stress latter via its C-terminal domain and regulates transport activity according to both stimuli. This intriguing sensing and regulation behavior of BetP was intensively studied in the past. It was shown by several biochemical studies that activation and regulation depends crucially on the lipid composition of the surrounding membrane. In fact, BetP is active and regulated only when negatively charged lipids are present. Recent structural studies have revealed binding of phosphatidylglycerol lipids to functional important parts of BetP, suggesting a functional role of lipid interactions. However, a regulatory role of lipid interactions could only be

SUBMITTER: Guler G 

PROVIDER: S-EPMC4813459 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature