Role of Phosphorylation in Moesin Interactions with PIP₂-Containing Biomimetic Membranes.

ABSTRACT: Moesin, a protein of the ezrin, radixin, and moesin family, which links the plasma membrane to the cytoskeleton, is involved in multiple physiological and pathological processes, including viral budding and infection. Its interaction with the plasma membrane occurs via a key phosphoinositide, the phosphatidyl(4,5)inositol-bisphosphate (PIP₂), and phosphorylation of residue T558, which has been shown to contribute, in cellulo, to a conformationally open protein. We study the impact of a double phosphomimetic mutation of moesin (T235D, T558D), which mimics the phosphorylation state of the protein, on protein/PIP₂/microtubule interactions. Analytical ultracentrifugation in the micromolar range showed moesin in the monomer and dimer forms, with wild-type (WT) moesin conta

SUBMITTER: Lubart Q 

PROVIDER: S-EPMC5912500 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature