RESUMO
Myosin VI (MVI), an actin-based molecular motor, is believed to have unique functions in eukaryotic cells, because it is the only myosin shown to move toward the pointed end of actin filaments, in the opposite direction of all other myosins. Given some unusual structural and kinetic properties of MVI, many models of its functioning in variety cellular processes have been proposed, and one of them is endocytosis. Different roles for many proteins associated with endocytic domains, such as clathrin or dynamin, have been defined. However, some results provide compelling evidence that actin filaments and MVI are both involved in two distinct steps of clathrin-dependent endocytosis: the formation of clathrin-coated vesicles and the movement of nascent uncoated vesicles from the actin-rich cell periphery to the early endosome. There are several postulated mechanisms of function for actin cytoskeleton and MVI during subsequent steps of clathrin-dependent endocytosis. Below we focus on their potential roles in this cellular process.
