Reference - Detail
|Author||Sabry JH, Moores SL, Ryan S, Zang JH, Spudich JA.|
|Title||Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells.|
|Journal||Mol. Biol. Cell|
Conventional myosin II plays a fundamental role in the process of cytokinesis where, in the form of bipolar thick filaments, it is thought to be the molecular motor that generates the force necessary to divide the cell. In Dictyostelium, the formation of thick filaments is regulated by the phosphorylation of three threonine residues in the tail region of the myosin heavy chain. We report here on the effects of this regulation on the localization of myosin in live cells undergoing cytokinesis. We imaged fusion proteins of the green-fluorescent protein with wild-type myosin and with myosins where the three critical threonines had been changed to either alanine or aspartic acid. We provide evidence that thick filament formation is required for the accumulation of myosin in the cleavage furrow and that if thick filaments are overproduced, this accumulation is markedly enhanced. This suggests that myosin localization in dividing cells is regulated by myosin heavy chain phosphorylation.
|MeSH||Actins / metabolism Amino Acid Substitution / genetics Animals Biological Transport Cell Division* Cell Movement Cell Nucleus / metabolism Cell Survival Cells, Cultured Dictyostelium / cytology* Dictyostelium / genetics Dictyostelium / metabolism* Gene Deletion Green Fluorescent Proteins Kinetics Luminescent Proteins / chemistry Luminescent Proteins / genetics Luminescent Proteins / metabolism Myosin Heavy Chains / chemistry Myosin Heavy Chains / genetics Myosin Heavy Chains / metabolism* Myosins / metabolism* Phosphorylation Phosphothreonine / metabolism Recombinant Fusion Proteins / chemistry Recombinant Fusion Proteins / genetics Recombinant Fusion Proteins / metabolism Threonine / genetics Threonine / metabolism|
|WOS Category||CELL BIOLOGY|
|Cellular slime molds||S00441 S00442|