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Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments

Abstract

The small GTPase Rho and one of its targets, Rho-associated kinase (Rho-kinase), are implicated in a wide spectrum of cellular functions, including cytoskeletal rearrangements, transcriptional activation and smooth muscle contraction. Since Rho also plays an essential role in cytokinesis, Rho-kinase may possibly mediate some biological aspects of cytokinesis. Here, using a series of monoclonal antibodies that can specifically recognize distinct phosphorylated sites on glial fibrillary acidic protein (GFAP) and vimentin, phosphorylation sites by Rho-kinase in vitro were revealed to be identical to in vivo phosphorylation sites on these intermediate filament (IF) proteins at the cleavage furrow in dividing cells. We then found, by preparing two types of anti-Rho-kinase antibodies, that Rho-kinase accumulated highly and circumferentially at the cleavage furrow in various cell lines. This subcellular distribution during cytokinesis was very similar to that of ezrin/radixin/moesin (ERM) proteins and Ser19-phosphorylated myosin light chain. These results raise the possibility that Rho-kinase might be involved in the formation of the contractile ring by modulating these F-actin-binding proteins during cytokinesis and in the phosphorylation and regulation of IF proteins at the cleavage furrow.

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References

  • Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, Matsuura Y and Kaibuchi K . 1996 J. Biol. Chem. 271: 20246–20249.

  • Amano M, Chihara K, Kimura K, Fukata Y, Nakamura N, Matsuura Y and Kaibuchi K . 1997 Science 275: 1308–1311.

  • Drechsel DN, Hyman AA, Hall A and Glotzer M . 1997 Curr. Biol. 7: 12–23.

  • Fukata Y, Kimura K, Oshiro N, Saya H, Matsuura Y and Kaibuchi K . 1998 J. Cell Biol. 141: 409–418.

  • Georgatos SD and Blobel G . 1987 J. Cell Biol. 105: 105-115.

  • Goto H, Kosako H, Tanabe K, Yanagida M, Sakurai M, Amano M, Kaibuchi K and Inagaki M . 1998 J. Biol. Chem. 273: 11728–11736.

  • Hall A . 1998 Science 279: 509–514.

  • Ho CL, Martys JL, Mikhailov A, Gundersen GG and Liem RKH . 1998 J. Cell Sci. 111: 1767–1778.

  • Hunt T . 1991 Semin. Cell Biol. 2: 213–222.

  • Huttenlocher A, Sandborg RR and Horwitz A . 1995 Curr. Opin. Cell Biol. 7: 697–706.

  • Inagaki M, Inagaki N, Takahashi T and Takai Y . 1997a J. Biochem. 121: 407–414.

  • Inagaki N, Goto H, Ogawara M, Nishi Y, Ando S and Inagaki M . 1997b J. Biol. Chem. 272: 25195–25199.

  • Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N and Narumiya S . 1996 EMBO J. 15: 1885–1893.

  • Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, Yamamori B, Feng J, Nakano T, Okawa K, Iwamatsu A and Kaibuchi K . 1996 Science 273: 245–248.

  • Kimura K, Fukata Y, Matsuoka Y, Bennett V, Matsuura Y, Okawa K, Iwamatsu A and Kaibuchi K . 1998 J. Biol. Chem. 273: 5542–5548.

  • Kishi K, Sasaki T, Kuroda S, Itoh T and Takai Y . 1993 J. Cell Biol. 120: 1187–1195.

  • Kosako H, Amano M, Yanagida M, Tanabe K, Nishi Y, Kaibuchi K and Inagaki M . 1997 J. Biol. Chem. 272: 10333–10336.

  • Leung T, Manser E, Tan L and Lim L . 1995 J. Biol. Chem. 270: 29051–29054.

  • Mabuchi I, Hamaguchi Y, Fujimoto H, Morii N, Mishima M and Narumiya S . 1993 Zygote 1: 325–331.

  • Madaule P, Eda M, Watanabe N, Fujisawa K, Matsuoka T, Bito H, Ishizaki T and Narumiya S . 1998 Nature 394: 491–494.

  • Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A and Kaibuchi K . 1996 EMBO J. 15: 2208–2216.

  • Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita Sa and Tsukita Sh . 1998 J. Cell Biol. 140: 647–657.

  • Matsumura F, Ono S, Yamakita Y, Totsukawa G and Yamashiro S . 1998 J. Cell Biol. 140: 119–129.

  • Matsuoka Y, Nishizawa K, Yano T, Shibata M, Ando S, Takahashi T and Inagaki M . 1992 EMBO J. 11: 2895–2902.

  • Nigg EA . 1993 Curr. Opin. Cell Biol. 5: 187–193.

  • Norbury C and Nurse P . 1992 Annu. Rev. Biochem. 61: 441–470.

  • Ogawara M, Inagaki N, Tsujimura K, Takai Y, Sekimata M, Ha MH, Imajoh-Ohmi S, Hirai S, Ohno S, Sugiura H, Yamauchi T and Inagaki M . 1995 J. Cell Biol. 131: 1055–1066.

  • Pines J . 1993 Trends Biochem. Sci. 18: 195–197.

  • Reed SI . 1992 Annu. Rev. Cell Biol. 8: 529–561.

  • Sato N, Yonemura S, Obinata T, Tsukita Sa and Tsukita Sh . 1991 J. Cell Biol. 113: 321–330.

  • Sekimata M, Tsujimura K, Tanaka J, Takeuchi Y, Inagaki N and Inagaki M . 1996 J. Cell Biol. 132: 635–641.

  • Sherr CJ . 1993 Cell 73: 1059–1065.

  • Takai Y, Ogawara M, Tomono Y, Moritoh C, Imajoh-Ohmi S, Tsutsumi O, Taketani Y and Inagaki M . 1996 J. Cell Biol. 133: 141–149.

  • Takaishi K, Sasaki T, Kameyama T, Tsukita Sa, Tsukita Sh and Takai Y . 1995 Oncogene 11: 39–48.

  • Tsujimura K, Ogawara M, Takeuchi Y, Imajoh-Ohmi S, Ha MH and Inagaki M . 1994 J. Biol. Chem. 269: 31097–31106.

  • Tsukita Sa, Yonemura S and Tsukita Sh . 1997 Trends Biochem. Sci. 22: 53–58.

  • Van Aelst L and D'Souza-Schorey C . 1997 Genes Dev. 11: 2295–2322.

  • Yasui Y, Amano M, Nagata K, Inagaki N, Nakamura H, Saya H, Kaibuchi K and Inagaki M . 1998 J. Cell Biol. 143: 1249–1258.

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Acknowledgements

We thank Drs S Yonemura and S Tsukita for providing anti-ERM mAb (CR22); Dr F Matsumura for providing anti-phosphorylated MLC-Ser19 (pp2b); N Takahashi for preparing GST-CAT; F Shigei for financial support to YT and TO; K Ando for technical assistance; K Kuromiya for the secretarial services and M Ohara for critique of the manuscript. This work was supported in part by Grants-in-Aid for Scientific Research and Cancer Research from the Ministry of Education, Science, Sports and Culture of Japan; Japan Society of the Promotion of Science Research for the Future; special coordination funds from the Science and Technology Agency of the Government of Japan; and a grant from Bristol-Myers-Squibb.

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Kosako, H., Goto, H., Yanagida, M. et al. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments. Oncogene 18, 2783–2788 (1999). https://doi.org/10.1038/sj.onc.1202633

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