Dynamic Lipid-dependent Modulation of Protein Topology by Post-translational Phosphorylation.

ABSTRACT: Membrane protein topology and folding are governed by structural principles and topogenic signals that are recognized and decoded by the protein insertion and translocation machineries at the time of initial membrane insertion and folding. We previously demonstrated that the lipid environment is also a determinant of initial protein topology, which is dynamically responsive to post-assembly changes in membrane lipid composition. However, the effect on protein topology of post-assembly phosphorylation of amino acids localized within initially cytoplasmically oriented extramembrane domains has never been investigated. Here, we show in a controlled in vitro system that phosphorylation of a membrane protein can trigger a change in topological arrangement. The rate of change occurred on a scale

SUBMITTER: Vitrac H 

PROVIDER: S-EPMC5290939 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature