In partnership with actin cytoskeletal filaments, at least 15 classes of myosins accomplish diverse tasks in cell motility such as muscle contraction, chemotaxis, cytokinesis, pinocytosis, targeted vesicle transport and, possibly, signal transduction (Mermall et al. 1998). Biochemical and mechanical studies have established the link between elementary events in the actomyosin ATPase cycle and work output (Cooke 1997), but the associated changes in molecular structure are still vague. X-ray crystallography (Rayment et al. 1996), in vitro mechanics of the purified proteins, mutagenesis (Sweeney and Holzbaur 1996), and time-resolved structural studies on muscle fibers (Irving and Piazzesi 1997) are providing new insights into this problem. Data from of all of these approaches must be integrated to understand energy transduction by motor proteins.
Yale E. Goldman (Wed,) studied this question.