RT Journal Article
SR Electronic
T1 The role of PLK1-phosphorylated SVIL in myosin II activation and cytokinetic furrowing
JF Journal of Cell Science
JO J. Cell Sci.
FD The Company of Biologists Ltd
SP 3627
OP 3637
DO 10.1242/jcs.124818
VO 126
IS 16
A1 Hasegawa, Hitoki
A1 Hyodo, Toshinori
A1 Asano, Eri
A1 Ito, Satoko
A1 Maeda, Masao
A1 Kuribayashi, Hirokazu
A1 Natsume, Atsushi
A1 Wakabayashi, Toshihiko
A1 Hamaguchi, Michinari
A1 Senga, Takeshi
YR 2013
UL http://jcs.biologists.org/content/126/16/3627.abstract
AB 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.