Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.

ABSTRACT: Endophilin is an N-BAR protein, which is characterized by a crescent-shaped BAR domain and an amphipathic helix that contributes to the membrane binding of these proteins. The exact function of that H0 helix has been a topic of debate. In mammals, there are five different endophilin isoforms, grouped into A (three members) and B (two members) subclasses, which have been described to differ in their subcellular localization and function. We asked to what extent molecular properties of the H0 helices of these members affect their membrane targeting behavior. We found that all H0 helices of the endophilin isoforms display a two-state equilibrium between disordered and α-helical states in which the helical secondary structure can be stabilized through trifluoroethanol. The helicities in high T

SUBMITTER: Robustelli J 

PROVIDER: S-EPMC8328966 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature