In contrast to the radial array of microtubules in most cultured cells, the microtubules in polarised epithelial cells are organised along the apico-basal axis, with microtubule minus-ends found at the apical side of the cell instead of at centrosomes. A picture of how the microtubule network is formed in these cells is beginning to emerge, with a key role for members of the calmodulin-regulated spectrin-associated protein (CAMSAP)/Patronin family of microtubule-minus-end decorating proteins. In this issue (p. 4278), Ivar Noordstra, Anna Akhmanova and colleagues investigate the mechanism by which CAMSAP3-bound microtubule minus-ends localise apically in human intestinal cells and describe an interaction of CAMSAP3 with the spektraplakin ACF7. Using 2D and 3D cultures of intestinal epithelial cells, the authors show that knockdown of ACF7, but not CAMSAP3, affects the formation of 3D cysts. However, the absence of CAMSAP3 induces a reversal from an apico-basal to a radial microtubule array. This causes clustering of Rab11A-positive endosomes in the pericentrosomal region, instead of their normal apical targeting, as well as misorganisation of the apical actin cytoskeleton. Taken together, the data presented here provide new insights into how microtubule organisation is controlled in intestinal cells and highlight ACF7 as an important regulator of epithelial cell polarity.