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

研究成果: ジャーナルへの寄稿学術論文査読

30 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)3627-3637
ページ数11
ジャーナルJournal of cell science
126
16
DOI
出版ステータス出版済み - 2013
外部発表はい

All Science Journal Classification (ASJC) codes

  • 細胞生物学

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