Understanding cellular and molecular components of cell migration is critical to the advancement of normal physiology and cancer biology. There is growing realization that finger-like cellular protrusions called filopodia play central roles in the cell biology underlying angiogenesis and inflammation (Anderson and Anderson, 1976; Gerhardt et al., 2003). Despite this knowledge, very little is known about the fundamental mechanisms governing filopodia formation, signaling, and adhesion. Unconventional myosins, particularly the MyTH4-FERM class of myosins, are implicated in precisely these types of filopodial functions (Tuxworth et al., 2001). Myosin-X (Myo10) is a vertebrate-specific member of the MyTH4-FERM class of myosins that is expressed in most cells and tissues. When expressed in cells, GFP-Myo10 displays a striking localization to tips of filopodia and undergoes intrafilopodial motility (Berg and Cheney, 2002). The experiments described in this dissertation demonstrate that Myo10 is a component of a putative filopodial tip complex, that it binds integrins (Zhang et al., 2004), and that it is a potent inducer of dorsal filopodia (Bohil et al., 2006)
