title: Initial diameter of the polar body contractile ring is minimized by the centralspindlin complex.
abstract: Polar body formation is an essential step in forming haploid eggs from diploid oocytes. This process involves completion of a highly asymmetric cytokinesis that results in a large egg and two small polar bodies. Unlike mitotic contractile rings, polar body contractile rings assemble over one spindle pole so that the spindle must move through the contractile ring before cytokinesis. During time-lapse imaging of C. elegans meiosis, the contractile ring moved downward along the length of the spindle and completed scission at the midpoint of the spindle, even when spindle length or rate of ring movement was increased. Patches of myosin heavy chain and dynamic furrowing of the plasma membrane over the entire embryo suggested that global cortical contraction forces the meiotic spindle and overlying membrane out through the contractile ring center. Consistent with this model, depletion of myosin phosphatase increased the velocity of ring movement along the length of the spindle. Global dynamic furrowing, which was restricted to anaphase I and II, was dependent on myosin II, the anaphase promoting complex and separase, but did not require cortical contact by the spindle. Large cortical patches of myosin during metaphase I and II indicated that myosin was already in the active form before activation of separase. To identify the signal at the midpoint of the anaphase spindle that induces scission, we depleted two proteins that mark the exact midpoint of the spindle during late anaphase, CYK-4 and ZEN-4. Depletion of either protein resulted in the unexpected phenotype of initial ingression of a polar body ring with twice the diameter of wild type. This phenotype revealed a novel mechanism for minimizing polar body size. Proteins at the spindle midpoint are required for initial ring ingression to occur close to the membrane-proximal spindle pole.
authors: Department of Molecular and Cellular Biology, 149 Briggs Hall, University of California, Davis, Davis, CA 95616, USA.
authors: Amy S
authors: AS
authors: Fabritius
authors: Department of Molecular and Cellular Biology, 149 Briggs Hall, University of California, Davis, Davis, CA 95616, USA.
authors: Jonathan R
authors: JR
authors: Flynn
authors: Department of Molecular and Cellular Biology, 149 Briggs Hall, University of California, Davis, Davis, CA 95616, USA. Electronic address: fjmcnally@ucdavis.edu.
authors: Francis J
authors: FJ
authors: McNally
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000196:embryology*; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000502:physiology*; D008869:Microtubule-Associated Proteins / Q000502:physiology*; D009218:Myosins / Q000502:physiology; D010750:Phosphoproteins / Q000502:physiology*; D034622:RNA Interference
chemical_list: D018797:Cell Cycle Proteins; D008869:Microtubule-Associated Proteins; D010750:Phosphoproteins; C104434:spindlin; D009218:Myosins