title: Regulation and control of myosin-I by the motor and light chain-binding domains.
abstract: Members of the myosin-I family of molecular motors are expressed in many eukaryotes, where they are involved in a multitude of critical processes. Humans express eight distinct members of the myosin-I family, making it the second largest family of myosins expressed in humans. Despite the high degree of sequence conservation in the motor and light chain-binding domains (LCBDs) of these myosins, recent studies have revealed surprising diversity of function and regulation arising from isoform-specific differences in these domains. Here we review the regulation of myosin-I function and localization by the motor and LCBDs.
authors.affiliation: The Pennsylvania Muscle Institute and Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Greenberg
authors.forename: E Michael
authors.initials: EM
authors.lastname: Ostap
mesh_terms: D000199:Actins / Q000737:chemistry; D000251:Adenosine Triphosphatases / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D001696:Biomechanical Phenomena; D002462:Cell Membrane / Q000737:chemistry*; D006801:Humans; D040542:Mechanotransduction, Cellular; D024461:Myosin Type I / Q000737:chemistry*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D020033:Protein Isoforms / Q000737:chemistry; D017434:Protein Structure, Tertiary; D021381:Protein Transport
chemical_list: D000199:Actins; D020033:Protein Isoforms; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D024461:Myosin Type I; C460367:MYO1C protein, human