title: The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing.
abstract: Polo-like kinase 1 (PLK1) is a widely conserved serine/threonine kinase that regulates progression of multiple stages of mitosis. Although extensive studies about PLK1 functions during cell division have been performed, it is still not known how PLK1 regulates myosin II activation at the equatorial cortex and ingression of the cleavage furrow. In this report, we show that an actin/myosin-II-binding protein, supervillin (SVIL), is a substrate of PLK1. PLK1 phosphorylates Ser238 of SVIL, which can promote the localization of SVIL to the central spindle and association with PRC1. Expression of a PLK1 phosphorylation site mutant, S238A-SVIL, inhibited myosin II activation at the equatorial cortex and induced aberrant furrowing. SVIL has both actin- and myosin-II-binding regions in the N-terminus. Expression of ΔMyo-SVIL (deleted of the myosin-II-binding region), but not of ΔAct-SVIL (deleted of actin-binding region), reduced myosin II activation and caused defects in furrowing. Our study indicates a possible role of phosphorylated SVIL as a molecular link between the central spindle and the contractile ring to coordinate the activation of myosin II for the ingression of the cleavage furrow.
authors.affiliation: Division of Cancer Biology, Nagoya University, Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya466-8550, Japan.
authors.forename: Hitoki
authors.initials: H
authors.lastname: Hasegawa
authors.forename: Toshinori
authors.initials: T
authors.lastname: Hyodo
authors.forename: Eri
authors.initials: E
authors.lastname: Asano
authors.forename: Satoko
authors.initials: S
authors.lastname: Ito
authors.forename: Masao
authors.initials: M
authors.lastname: Maeda
authors.forename: Hirokazu
authors.initials: H
authors.lastname: Kuribayashi
authors.forename: Atsushi
authors.initials: A
authors.lastname: Natsume
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Wakabayashi
authors.forename: Michinari
authors.initials: M
authors.lastname: Hamaguchi
authors.forename: Takeshi
authors.initials: T
authors.lastname: Senga
mesh_terms: D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D048749:Cytokinesis / Q000502:physiology; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism*; D024462:Myosin Type II / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000235:genetics / Q000378:metabolism*; D008941:Spindle Apparatus / Q000378:metabolism*; D014162:Transfection; D000097869:Polo-Like Kinase 1
chemical_list: D018797:Cell Cycle Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins; D024462:Myosin Type II; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D000097869:Polo-Like Kinase 1; C109413:SVIL protein, human
keywords: Central spindle; Cytokinesis; PLK1; Phosphorylation; SVIL