A mutational analysis of the endophilin-A N-BAR domain performed in living flies.

ABSTRACT:

Background

Endophilin is a cytoplasmic protein with an important function in clathrin-dependent endocytosis at synapses and elsewhere. Endophilin has a BAR (Bin/Amphiphysin/Rvs-homology) domain, which is implicated in the sensing and induction of membrane curvature. Previous structure-function studies of the endophilin-A BAR domain have almost exclusively been made in reduced systems, either in vitro or ex vivo in cultured cells. To extend and complement this work, we have analyzed the role played by the structural features of the endophilin-A BAR domain in Drosophila in vivo.

Methodology/principal findings

The study is based on genetic rescue of endophilin-A (endoA) null mutants with wild type or mutated endoA transgenes. We evaluated the viability of the rescuants, the loc

SUBMITTER: Jung AG 

PROVIDER: S-EPMC2831065 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature