The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing

Hitoki Hasegawa, Toshinori Hyodo, Eri Asano, Satoko Ito, Masao Maeda, Hirokazu Kuribayashi, Atsushi Natsume, Toshihiko Wakabayashi, Michinari Hamaguchi, Takeshi Senga

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19 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3627-3637
Number of pages11
JournalJournal of cell science
Volume126
Issue number16
DOIs
Publication statusPublished - 2013

All Science Journal Classification (ASJC) codes

  • Cell Biology

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    Hasegawa, H., Hyodo, T., Asano, E., Ito, S., Maeda, M., Kuribayashi, H., Natsume, A., Wakabayashi, T., Hamaguchi, M., & Senga, T. (2013). The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing. Journal of cell science, 126(16), 3627-3637. https://doi.org/10.1242/jcs.124818