title: Reflections on a quarter century of research on contractile systems.
abstract: By the early 1970s studies of muscle contraction reached a high level and the field gave birth to a new line of investigation into the molecular basis of cellular movements. The molecular diversity in these motile systems has proven to be greater than anticipated. Actin filament assembly without direct participation of myosin is used more widely for motility than expected. Atomic structures of key proteins and important technical advances, including single-molecule methods, have enabled detailed investigation of the mechanisms of muscle contraction and cellular motility. However, much work lies ahead to understand the mechanism of force production and to elucidate the signaling pathways that control cellular motility.
authors: Structural Biology Laboratory, Salk Institute for Biological Studies, 10010 N. Torrey Pines Road, La Jolla, CA 92037, USA. pollard@salk.edu
authors: T D
authors: TD
authors: Pollard
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D006801:Humans; D008967:Molecular Biology / Q000639:trends*; D009119:Muscle Contraction / Q000502:physiology*; D009124:Muscle Proteins / Q000378:metabolism; D012106:Research / Q000639:trends*; D012518:Sarcomeres / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D000199:Actins; D009124:Muscle Proteins