Roles of Rho-associated kinase in cytokinesis; mutations in Rho- associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments

Journal of Cell Biology

Volumn 143, Issue 5, 1998, Pages 1249-1258

  Yasui, Yoshihiro ^a   Amano, Mutsuki ^b   Nagata, Koh Ichi ^a   Inagaki, Naoyuki ^a   Nakamura, Hideo ^c   Saya, Hideyuki ^c   Kaibuchi, Kozo ^b   Inagaki, Masaki ^a  

^a AICHI CANCER CENTER HOSPITAL   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^c KUMAMOTO UNIVERSITY   (Japan)

Author keywords

Cytokinesis; Glial fibrillary acidic protein (GFAP); Intermediate filament; Rho; Rho associated kinase

Indexed keywords

ADDUCIN; EZRIN; GLIAL FIBRILLARY ACIDIC PROTEIN; GUANOSINE TRIPHOSPHATASE; INTERMEDIATE FILAMENT PROTEIN; MOESIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN KINASE; RADIXIN; RHO FACTOR; RHO KINASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CYTOKINESIS; CYTOPLASM; CYTOSKELETON; EMBRYO; GENE MUTATION; HUMAN; HUMAN CELL; INTERMEDIATE FILAMENT; MAMMAL CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; CATALYTIC DOMAIN; CELL DIVISION; CYTOSKELETON; FEMALE; GLIAL FIBRILLARY ACIDIC PROTEIN; INTERMEDIATE FILAMENTS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; L CELLS (CELL LINE); MICE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; TRANSFECTION; XENOPUS;

ANIMALIA; MAMMALIA; XENOPUS LAEVIS;

EID: 0032583123     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.5.1249     Document Type: Article

References (41)

1. Amano, M., H. Mukai, Y. Ono, K. Chihara, T. Matsui, Y. Hamajima, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996a. Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science. 271: 648-650.
2. Amano, M., M. Ito, K. Kimura, Y. Fukata, K. Chihara, T. Nakano, Y. Matsuura, and K. Kaibuchi. 1996b. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271:20246-20249.
3. Amano, M., K. Chihara, K. Kimura, Y. Fukata, N. Nakamura, Y. Matsuura, and K. Kaibuchi. 1997. Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science. 275:1308-1311.
4. Amano, M., K. Chihara, N. Nakamura, Y. Fukata, T. Yano, M. Shibata, M. Ikebe, and K. Kaibuchi. 1998. Myosin II activation promotes neurite retraction during the action of Rho and Rho-kinase. Genes Cells. 3:177-188.
5. Chihara, K., M. Amano, N. Nakamura, T. Yano, T. Shibata, T. Tokui, H. Ichikawa, R. Ikebe, M. Ikebe, and K. Kaibuchi. 1997. Cytoskeletal rearrangements and transcriptional activation of c-fos serum response element by Rho-kinase. J. Biol. Chem. 272:25121-25127.
6. Chou, Y.-H., P. Opal, R.A. Quinlan, and R.D. Goldman. 1996. The relative roles of specific N-and C-terminal phosphorylation sites in the disassembly of intermediate filament in mitotic BHK-21 cells. J. Cell Sci. 109:817-826.
7. Drechsel, D.N., A.A. Hyman, A. Hall, and M. Glotzer. 1996. A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr. Biol. 7:12-23.
8. Eriksson, J.E., P. Opal, and R.D. Goldman. 1992. Intermediate filament dynamics. Curr. Opin. Cell Biol. 4:99-104.
9. Farah, S., Y. Agazie, N. Ohan, J.K. Ngsee, and X.J. Liu. 1998. A rho-associated protein kinase, ROKalpha, binds insulin receptor substrate-1 and modulates insulin signaling. J. Biol. Chem. 273:4740-4746.
10. Fuchs, E., and K. Weber. 1994. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63:345-382.
11. Fukata, Y., K. Kimura, N. Oshiro, H. Saya, Y. Matsuura, and K. Kaibuchi. 1998. Association of the myosin-binding subunit of myosin phosphatase and moesin: dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase. J. Cell. Biol. 141:409-418.
12. Goto, H., H. Kosako, K. Tanabe, M. Yanagida, M. Sakurai, M. Amano., K. Kaibuchi, and M. Inagaki. 1998. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J. Biol. Chem. 273:11728-11736.
13. Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science. 279:509-514.
14. Heald, R., and F. McKeon. 1990. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell. 61:579-589.
15. Hunt, T. 1991. Cyclins and their partners: from a simple idea to complicated reality. Semin. Cell Biol. 2:213-222.
16. Inagaki, M., Y. Matsuoka, K. Tsujimura, S. Ando, T. Tokui, T. Takahashi, and N. Inagaki. 1996. Dynamic property of intermediate filaments: regulation by phosphorylation. Bioessays. 18:481-487.
17. Ishizaki, T., M. Naito, K. Fujisawa, M. Maekawa, N. Watanabe, Y. Saito, and S. Narumiya. 1997. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induce focal adhesions. FEBS (Fed. Eur. Biochem. Soc.) Lett. 404:118-124.
18. Kimura, K., M. Ito, M. Amano, K. Chihara, Y. Fukata, M. Nakafuku, B. Yamamori, J. Feng, T. Nakano, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science. 273:245-248.
19. Kimura, K., Y. Fukata, Y. Matsuoka, V. Bennett, Y. Matsuura, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1998. Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J. Biol. Chem. 273:5542-5548.
20. Kishi, K., T. Sasaki, S. Kuroda, T. Itoh, and Y. Takai. 1993. Regulation of cytoplasmic division of Xenopus cbryo by rho p21 and its inhibitory GDP/GTP exchange protein (rhoGDI). J. Cell Biol. 120:1187-1195.
21. Kosako, H., M. Amano, M. Yanagida, K. Tanabe, Y. Nishi, K. Kaibuchi, and M. Inagaki. 1997. Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. J. Biol. Chem. 272:10333-10336.
22. Kosako, H., H. Goto, M. Yanagida, K. Matsuzawa, M. Fujita, Y. Tomono, T. Okigaki, H. Odai, K. Kaibuchi, and M. Inagaki. 1998. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments. Oncogene. In press.
23. Kureishi, Y., S. Kobayashi, M. Amano, K. Kimura, H. Kanaide, T. Nakano, K. Kaibuchi, and M. Itoh. 1997. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272:12257-12260.
24. Leung, T., X.-Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
25. Leung, T., X.-Q. Chen, I. Tan, E. Manser, and L. Lim. 1998. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol. Cell. Biol. 18:130-140.
26. Mabuchi, I., Y. Hamaguchi, H. Fujimoto, N. Morii, M. Mishima, and S. Narumiya. 1993. A rho-like protein is involved in the organization of the contractile ring in dividing sand dollar eggs. Zygote. 1:325-331.
27. Machesky, L.M., and A. Hall. 1996. Rho: a connection between membrane receptor signaling and the cytoskeleton. Trends Cell Biol. 6:304-310.
28. Matsui, T., M. Amano, T. Yamamoto, K. Chihara, M. Nakafuku, M. Ito, T. Nakano, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO (Eur. Mol. Biol. Organ.) J. 15:2208-2216.
29. Matsui, T., M. Maeda, Y. Doi, S. Yonemura, M. Amano, K. Kaibuchi, S. Tsukita, and Sh. Tsukita. 1998. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140:647-657.
30. Matsuoka, Y., K. Nishizawa, T. Yano, M. Shibata, S. Ando, T. Takahashi, and M. Inagaki. 1992. Two different protein kinases act on a different time schedule as glial filament kinases during mitosis. EMBO (Eur. Mol. Biol. Organ.) J. 11:2895-2902.
31. Mukai, H., and Y. Ono. 1994. A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. Biochem. Biophys. Res. Commun. 199:897-904.
32. Murray, A., and T. Hunt. 1993. The Cell Cycle: An Introduction. Oxford University Press, Oxford, UK. 42-56.
33. Nigg, E.A. 1993. Targets of cyclin-dependent protein kinases. Curr. Opin. Cell Biol. 5:187-193.
34. Nishizawa, K., T. Yano, M. Shibata, S. Ando, S. Saga, T. Takahashi, and M. Inagaki. 1991. Specific localization of phosphointermediate filament protein in the constricted area of dividing cells. J. Biol. Chem. 266:3074-3079.
35. Norbury, C., and P. Nurse. 1992. Animal cell cycles and their control. Annu. Rev. Biochem. 61:441-470.
36. Reeves, S.A., L.J. Helman, A. Allison, and M.A. Israel. 1989. Molecular cloning and primary structure of human glial fibrillary acidic protein. Proc. Natl. Acad. Sci. USA. 86:5178-5182.
37. Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. Phosphorylation of myosin-II regulatory light chain by cyclin-p34cdc2: a mechanism for the timing of cytokinesis. J. Cell Biol. 118:595-605.
38. Sekimata, M., K. Tsujimura, J. Tanaka, Y. Takeuchi, N. Inagaki, and M. Inagaki. 1996. Detection of protein kinase activity specifically activated at metaphase-anaphase transition. J. Cell Biol. 132:635-641.
39. Takaishi, K., T. Sasaki, T. Kameyama, S. Tsukita, Sh. Tsukila, and Y. Takai. 1995. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:39-48.
40. Watanabe, G., Y. Saito, P. Madaule, T. Ishizaki, K, Fujisawa, N. Morii, H. Mukai, Y. Ono, A. Kakizuka, and S. Narumiya. 1996. Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science. 271:645-648.
41. Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells. J. Cell Biol. 124:129-137.