Many mature epithelia have apical brush borders made from densely packed microvilli. These are supported by F-actin bundles linked by a terminal web of spectrin and myosin II. How the vesicles that maintain the brush border move through this dense network is unclear. On p. 1361, Matthew Phillips and Graham Thomas propose that brush border spectrin - βHeavy-spectrin - helps vesicles to make this journey, showing that it is required for early endosome recycling in Drosophila intestinal cells. They show that endosomes bearing the GTPase Rab5 are defective in the cuprophilic cells of the larval midgut of karst mutants, which lack functional βHeavy-spectrin. They also find that brush borders and early endosomes from these mutants lack the apical H+ V-ATPase that is normally present. This loss seems to disrupt normal acid secretion from the cuprophilic cells. Finally, the authors use epistasis experiments to place βHeavy- spectrin between dynamin and Rab5-dependent endosome activities, which leads them to propose that spectrin `primes' newly internalized proteins so that they can navigate the terminal web and enter the recycling pathway at the early endosome.