title: Actin polymerization driven mitochondrial transport in mating S. cerevisiae.
abstract: The dynamic microenvironment of cells depends on macromolecular architecture, equilibrium fluctuations, and nonequilibrium forces generated by cytoskeletal proteins. We studied the influence of these factors on the motions of mitochondria in mating S. cerevisiae using Fourier imaging correlation spectroscopy (FICS). Our measurements provide detailed length-scale dependent information about the dynamic behavior of mitochondria. We investigate the influence of the actin cytoskeleton on mitochondrial motion and make comparisons between conditions in which actin network assembly and disassembly is varied either by using disruptive pharmacological agents or mutations that alter the rates of actin polymerization. Under physiological conditions, nonequilibrium dynamics of the actin cytoskeleton leads to 1.5-fold enhancement of the long-time mitochondrial diffusion coefficient and a transient subdiffusive temporal scaling of the mean-square displacement (MSD proportional, variant tau (alpha), with alpha = 2/3). We find that nonequilibrium forces associated with actin polymerization are a predominant factor in driving mitochondrial transport. Moreover, our results lend support to an existing model in which these forces are directly coupled to mitochondrial membrane surfaces.
authors.affiliation: Department of Chemistry, Oregon Center for Optics, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
authors.forename: Eric N
authors.initials: EN
authors.lastname: Senning
authors.forename: Andrew H
authors.initials: AH
authors.lastname: Marcus
mesh_terms: D000199:Actins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology; D002462:Cell Membrane / Q000502:physiology / Q000648:ultrastructure; D003599:Cytoskeleton / Q000502:physiology / Q000648:ultrastructure; D005583:Fourier Analysis; D007700:Kinetics; D008856:Microscopy, Fluorescence; D008870:Microtubules / Q000502:physiology / Q000648:ultrastructure; D008928:Mitochondria / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics* / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000199:Actins; D029701:Saccharomyces cerevisiae Proteins