Temporal Control of Contractile Ring Assembly by Plo1 Regulation of Myosin II Recruitment by Mid1/Anillin
In eukaryotes, cytokinesis generally involves an actomyosin ring, the contraction of which promotes daughter cell segregation. Assembly of the contractile ring is tightly controlled in space and time [1–4]. In the fission yeast, contractile ring components are first organized by the anillin-like pro...
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Published in | Current biology Vol. 21; no. 6; pp. 473 - 479 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
22.03.2011
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | In eukaryotes, cytokinesis generally involves an actomyosin ring, the contraction of which promotes daughter cell segregation. Assembly of the contractile ring is tightly controlled in space and time [1–4]. In the fission yeast, contractile ring components are first organized by the anillin-like protein Mid1 into medial cortical nodes [5–9]. These nodes then coalesce laterally into a functional contractile ring [10–13]. Although Mid1 is present at the medial cortex throughout G2 [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 is known to activate Mid1 nuclear export at mitotic onset [15, 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.
▸ Mid1 has at least two Plo1 binding sites, and the interaction is favored by Cdc2 ▸ Plo1 phosphorylates multiple residues within the first 100 residues of Mid1 ▸ Phosphorylation of Mid1 1–100 by Plo1 modulates the timing of myosin II recruitment ▸ Mid1 1–100 interacts with a Rng2 fragment |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 PMCID: PMC3088474 current address: Institut Cochin, Institut Cochin, Inserm U1016, CNRS UMR8104, Université Paris Descartes, 75014 Paris, France. |
ISSN: | 0960-9822 1879-0445 |
DOI: | 10.1016/j.cub.2011.02.003 |