Abstract
Myosin-1a is one of eight monomeric, membrane binding class I myosins expressed in vertebrates.1 As the most abundant actin-based motor protein found in the enterocyte microvillus, myosin-1a has long been known to interact with the apical membrane via a highly basic C-terminal tail domain.2 Several recent studies shed light on possible functional consequences of this protein/lipid interaction. In vitro and in vivo studies of microvillar function have revealed that myosin-1a can move apical membrane along core actin bundles, leading to the release of small vesicles from microvillar tips.3,4 Additional studies indicate that myosin-1a and other class I myosins contribute to membrane-cytoskeleton adhesion, which enables the apical membrane to resist deformation.5 These findings clearly position myosin-1a as an important player in apical membrane movement and structural stability. How this motor is able to fulfill these two seemingly distinct functions is currently unclear, but will serve as the focus of our discussion below.