A V0-ATPase-dependent apical trafficking pathway maintains the polarity of the intestinal absorptive membrane.

ABSTRACT: Intestine function relies on the strong polarity of intestinal epithelial cells and the array of microvilli forming a brush border at their luminal pole. Combining a genetic RNA interference (RNAi) screen with in vivo super-resolution imaging in the Caenorhabditiselegans intestine, we found that the V0 sector of the vacuolar ATPase (V0-ATPase) controls a late apical trafficking step, involving Ras-related protein 11 (RAB-11)⁺ endosomes and the N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE) synaptosome-associated protein 29 (SNAP-29), and is necessary to maintain the polarized localization of both apical polarity modules and brush border proteins. We show that the V0-ATPase pathway also genetically interacts with glycosphingolipi

SUBMITTER: Bidaud-Meynard A 

PROVIDER: S-EPMC7376742 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature