A primary function of the lining surface of the intestine is to absorb nutrients. The epithelial cells that form this surface are notable for the presence of a brush border composed of microvilli, tiny plasma membrane projections that markedly increase the surface area through which absorption can take place. The core of each microvillus is a bundle of 20 to 30 filaments of actin protein. At the outer tip of the bundle is a cluster of proteins known as the intermicrovillar adhesion complex (IMAC). The purpose of this complex is to connect the actin bundle to cadherin proteins in the plasma membrane at the tip of the microvillus. The cadherins then link the tips of adjacent microvilli together forming a well-organized lawn. An ongoing mystery regarding microvillus formation concerns how the IMAC proteins become localized at the tip of the actin bundle. This led Vanderbilt Basic Sciences investigator Matt Tyska and his laboratory to study the role of IMAC protein myosin-7b. They found that this protein is absolutely required for IMAC organization and adhesion of adjacent microvilli. Their studies suggest that myosin-7b’s ability to use the energy from ATP hydrolysis to transport cargo proteins along an actin filament enables it to transport IMAC proteins to the tip. In addition, myosin-7b contains protein interaction domains that can bind to other IMAC proteins, retaining them in the correct location and orientation. The results show that microvilli, like similar actin filament-based structures in other tissues and organisms, depend on a myosin family protein for correct structural organization. They also provide key information to aid in our understanding of brush border morphogenesis. The work is published in the journal Current Biology [M. L. Weck, et al. (2016), Curr. Biol., http://dx.doi.org/10.1016/j.cub.2016.08.014 ].