The endophilin curvature-sensitive motif requires electrostatic guidance to recycle synaptic vesicles in vivo.

ABSTRACT: Curvature-sensing mechanisms assist proteins in executing particular actions on various membrane organelles. Here, we investigate the functional specificity of curvature-sensing amphipathic motifs in Caenorhabditis elegans through the study of endophilin, an endocytic protein for synaptic vesicle recycling. We generate chimeric endophilin proteins by replacing the endophilin amphipathic motif H0 with other curvature-sensing amphipathic motifs. We find that the role of amphipathic motifs cannot simply be extrapolated from the identity of their parental proteins. For example, the amphipathic motif of the nuclear pore complex protein NUP133 functionally replaces the synaptic role of endophilin H0. Interestingly, non-functional endophilin chimeras have similar defects-producing fewer synaptic

SUBMITTER: Zhang L 

PROVIDER: S-EPMC8969179 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature