Temporal Control of Contractile Ring Assembly by Plo1 Regulation of Myosin II Recruitment by Mid1/Anillin
Autor: | Maria Almonacid, Damarys Loew, Jun-Song Chen, Anne Paoletti, Séverine Celton-Morizur, Adeline Mayeux, Dawn M. Clifford, Kathleen L. Gould, Jennifer L. Jakubowski, Florent Dingli |
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Přispěvatelé: | Centre interdisciplinaire de recherche en biologie (CIRB), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Collège de France (CdF)-PSL Research University (PSL), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Institut Curie, Laboratoire de Spectrométrie de Masse Protéomique, Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Labex MemoLife, École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Collège de France (CdF (institution))-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Institut Curie [Paris] |
Rok vydání: | 2011 |
Předmět: |
Cell division
Medial cortex [SDV]Life Sciences [q-bio] Protein Serine-Threonine Kinases Biology Time-Lapse Imaging Mass Spectrometry Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Contractile Proteins 0302 clinical medicine CDC2 Protein Kinase Schizosaccharomyces Myosin Immunoprecipitation Phosphorylation Nuclear export signal Mitosis ComputingMilieux_MISCELLANEOUS Cytokinesis 030304 developmental biology Myosin Type II 0303 health sciences Cyclin-dependent kinase 1 Binding Sites Agricultural and Biological Sciences(all) Biochemistry Genetics and Molecular Biology(all) Actomyosin Cell biology Microscopy Fluorescence Schizosaccharomyces pombe Proteins General Agricultural and Biological Sciences 030217 neurology & neurosurgery Plasmids |
Zdroj: | Current Biology-CB Current Biology-CB, Elsevier, 2011, 21 (6), pp.473-479. ⟨10.1016/j.cub.2011.02.003⟩ |
ISSN: | 0960-9822 1879-0445 |
Popis: | In eukaryotes, cytokinesis generally involves an acto-myosin ring, the contraction of which promotes daughter cells segregation. Assembly of the contractile ring is tightly controlled in space and time (see[1–4] for reviews). In the fission yeast, contractile ring components are first organized by the Anillin-like protein Mid1 [5, 6] and Cdr2 kinase [7–9] into medial cortical nodes. These nodes then coalesce laterally into a functional compact contractile ring [10–13]. Although Mid1 is present at the medial cortex throughout G2 phase [14], recruitment of contractile ring components to nodes starts only at mitotic onset [12] indicating that this event is cell cycle regulated. Polo kinases are key temporal coordinators of mitosis and cytokinesis [1] and the Polo-like kinase Plo1 [15] has long been implicated in Mid1 regulation [16]: Plo1 activates Mid1 nuclear export at mitotic onset [16], coupling division plane specification to nuclear position [7]. Here, we provide evidence that Plo1 also triggers the recruitment of contractile ring components into medial cortical nodes. Plo1 binds at least two independent sites on Mid1, including a consensus site phosphorylated by Cdc2. Plo1 phosphorylates several residues within the first 100 amino acids of Mid1, which directly interact with the IQGAP Rng2 [17], and influences the timing of Myosin II recruitment. Plo1 thereby facilitates contractile ring assembly at mitotic onset. |
Databáze: | OpenAIRE |
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