MYO7B is an actin-based motor protein that functions primarily in epithelial brush border organization and morphogenesis. As a core component of the intermicrovillar adhesion complex (IMAC), MYO7B localizes to microvillar tips where it promotes the accumulation and stabilization of cadherin-based adhesion links between adjacent microvilli 1. MYO7B accomplishes this through its MyTH4-FERM cargo-binding domain, which interacts with scaffolding proteins USH1C and ANKS4B to link protocadherins (CDHR2/CDHR5) to the actin cytoskeleton 23. Motor activity combined with passive targeting mechanisms drives highly efficient tip-directed transport of IMAC components 1. Loss of MYO7B disrupts intermicrovillar adhesion and mislocalized IMAC components along the microvillar axis, preventing proper brush border assembly in intestinal and kidney epithelial cells 1. Beyond epithelial morphogenesis, MYO7B regulates endocytosis by maintaining plasma membrane-associated actin networks that control clathrin-coated pit severing, particularly for heparan sulfate proteoglycan-binding cargos including α-synuclein fibrils 4. The structural and functional homology between MYO7B-containing complexes and MYO7A-based stereocilial complexes suggests shared mechanisms relevant to understanding Usher syndrome and sensory deficits 3.