title: Vesicle transport: the role of actin filaments and myosin motors.
abstract: The transport of vesicles and the retention of organelles at specific locations are fundamental processes in cells. Actin filaments and myosin motors have been shown to be required for both of these tasks. Most of the organelles in cells associate with actin filaments and some of the myosin motors required for movement on actin filaments have been identified. Myosin V has been shown to transport endoplasmic reticulum (ER) vesicles in neurons, pigment granules in melanocytes, and the vacuole in yeast. Myosin I has been shown to be involved in the transport of Golgi-derived vesicles in epithelial cells. Myosin VI has been shown to be associated with Golgi-derived vesicles, and cytoplasmic vesicles in living Drosophila embryos. Myosin II may be a vesicle motor but its role in vesicle transport has not been resolved. Secretory vesicles, endosomes and mitochondria appear to be transported on actin filaments but the myosin motors on these organelles have not been identified. Mitochondria in yeast may be transported by the dynamic assembly of an actin "tail." The model that has unified all of these findings is the concept that long-range movement of vesicles occurs on microtubules and short-range movement on actin filaments. The details of how the microtubule-dependent and the actin-dependent motors are coordinated are important questions in the field. There is now strong evidence that two molecular motors, kinesin and myosin V, interact with each other and perhaps function as a complex on vesicles. An understanding of the interrelationship of microtubules and actin filaments and the motors that move cargo on them will ultimately establish how vesicles and organelles are transported to their specific locations in cells.
authors.affiliation: Department of Biological Sciences, Dartmouth College, Hanover, New Hampshire 03755-3576, USA.
authors.forename: A S
authors.initials: AS
authors.lastname: DePina
authors.forename: G M
authors.initials: GM
authors.lastname: Langford
mesh_terms: D000199:Actins / Q000378:metabolism / Q000502:physiology*; D000818:Animals; D001369:Axons / Q000648:ultrastructure; D002148:Calmodulin-Binding Proteins / Q000502:physiology; D003599:Cytoskeleton / Q000737:chemistry* / Q000648:ultrastructure; D049832:Decapodiformes / Q000033:anatomy & histology; D004721:Endoplasmic Reticulum / Q000502:physiology; D011992:Endosomes; D006056:Golgi Apparatus / Q000502:physiology; D007150:Immunohistochemistry; D016547:Kinesins / Q000648:ultrastructure; D008247:Lysosomes / Q000502:physiology; D020460:Melanosomes / Q000502:physiology; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D008928:Mitochondria / Q000502:physiology; D020409:Molecular Motor Proteins / Q000502:physiology*; D018995:Myosin Heavy Chains / Q000502:physiology; D024701:Myosin Type V; D009218:Myosins / Q000502:physiology*; D009419:Nerve Tissue Proteins / Q000502:physiology; D015388:Organelles / Q000378:metabolism
chemical_list: D000199:Actins; D002148:Calmodulin-Binding Proteins; D020409:Molecular Motor Proteins; D009419:Nerve Tissue Proteins; C078829:chicken brain myosin-V p190; C089785:myosin VI; D024701:Myosin Type V; D018995:Myosin Heavy Chains; D009218:Myosins; D016547:Kinesins