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Vol. 16, Issue 8, 3865-3872, August 2005
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* Graduate School of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan;
Gene Function Research Center, National Institute for Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8562, Japan
Submitted March 20, 2005;
Accepted May 25, 2005
Monitoring Editor: John Pringle
Myosin II-dependent contraction of the contractile ring drives equatorial furrowing during cytokinesis in animal cells. Nonetheless, myosin II-null cells of the cellular slime mold Dictyostelium divide efficiently when adhering to substrates by making use of polar traction forces. Here, we show that in the presence of 30 µM blebbistatin, a potent myosin II inhibitor, normal rat kidney (NRK) cells adhering to fibronectin-coated surfaces formed equatorial furrows and divided in a manner strikingly similar to myosin II-null Dictyostelium cells. Such blebbistatin-resistant cytokinesis was absent in partially detached NRK cells and was disrupted in adherent cells if the advance of their polar lamellipodia was disturbed by neighboring cells. Y-27632 (40 µM), which inhibits Rho-kinase, was similar to 30 µM blebbistatin in that it inhibited cytokinesis of partially detached NRK cells but only prolonged furrow ingression in attached cells. In the presence of 100 µM blebbistatin, most NRK cells that initiated anaphase formed tight furrows, although scission never occurred. Adherent HT1080 fibrosarcoma cells also formed equatorial furrows efficiently in the presence of 100 µM blebbistatin. These results provide direct evidence for adhesion-dependent, contractile ring-independent equatorial furrowing in mammalian cells and demonstrate the importance of substrate adhesion for cytokinesis.
Abbreviations used: NRK, normal rat kidney; ROCK, Rho-kinase).
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Taro Q.P. Uyeda (t-uyeda{at}aist.go.jp).
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