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Volumn 162, Issue 2, 2003, Pages 223-232

Activity of Rho-family GTPases during cell division as visualized with FRET-based probes

Author keywords

Cdc42 GTP binding protein; Cytokinesis; Fluorescent probes; Rac GTP binding proteins; Rho GTP binding proteins

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42; RAC1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0042672950     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200212049     Document Type: Article
Times cited : (356)

References (47)
  • 1
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L., and A. Hall. 2000. Rho GTPases and their effector proteins. Biochem. J. 348:241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 2
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformiry gene
    • Castrillon, D.H., and S.A. Wasserman. 1994. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformiry gene. Development. 120:3367-3377.
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 4
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • Drechsel, D.N., A.A. Hyman, A. Hall, and M. Glotzer. 1997. A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr. Biol. 7:12-23.
    • (1997) Curr. Biol. , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 5
    • 0030022232 scopus 로고    scopus 로고
    • Cytokinesis arrest and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase CDC42Hs
    • Dutartre, H., J. Davoust, J.P. Gorvel, and P. Chavrier. 1996. Cytokinesis arrest and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase CDC42Hs. J. Cell Sci. 109:367-377.
    • (1996) J. Cell Sci. , vol.109 , pp. 367-377
    • Dutartre, H.1    Davoust, J.2    Gorvel, J.P.3    Chavrier, P.4
  • 6
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzera
    • Etienne-Manneville, S., and A. Hall. 2001. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzera. Cell. 106:489-498.
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 7
    • 0032987720 scopus 로고    scopus 로고
    • Video-rate scanning two-photon excitation fluorescence microscopy and ratio imaging with cameleons
    • Fan, G.Y., H. Fujisaki, A. Miyawaki, R.K. Tsay, R.Y. Tsien, and M.H. Ellisman. 1999. Video-rate scanning two-photon excitation fluorescence microscopy and ratio imaging with cameleons. Biophys. J. 76:2412-2420.
    • (1999) Biophys. J. , vol.76 , pp. 2412-2420
    • Fan, G.Y.1    Fujisaki, H.2    Miyawaki, A.3    Tsay, R.K.4    Tsien, R.Y.5    Ellisman, M.H.6
  • 8
    • 0023715225 scopus 로고
    • Inhibition of NIH3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP
    • Feig, L.A., and G.M. Cooper. 1988. Inhibition of NIH3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol. Cell. Biol. 8:3235-3243.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 10
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R., and R.Y. Tsien. 1996. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6:178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 11
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., G. Horn, M. Spaargaren, and A. Wittinghofer. 1996. Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271:6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 12
    • 0035937180 scopus 로고    scopus 로고
    • MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody
    • Hirose, K., T. Kawashima, I. Iwamoto, T. Nosaka, and T. Kitamura. 2001. MgcRacGAP is involved in cytokinesis through associating with mitotic spindle and midbody. J. Biol. Chem. 276:5821-5828.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5821-5828
    • Hirose, K.1    Kawashima, T.2    Iwamoto, I.3    Nosaka, T.4    Kitamura, T.5
  • 13
    • 0036724188 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 video-imaged by FRET-based single-molecule probes in the membrane of living cells
    • Itoh, R.E., K. Kurokawa, Y. Ohba, H. Yoshizaki, N. Mochizuki, and M. Matsuda. 2002. Activation of Rac and Cdc42 video-imaged by FRET-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22:6582-6591.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 14
    • 0034625353 scopus 로고    scopus 로고
    • Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation
    • Kimura, K., T. Tsuji, Y. Takada, T. Miki, and S. Narumiya. 2000. Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation. J. Biol. Chem. 275:17233-17236.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17233-17236
    • Kimura, K.1    Tsuji, T.2    Takada, Y.3    Miki, T.4    Narumiya, S.5
  • 15
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi, K., T. Sasaki, S. Kuroda, T. Itoh, and Y. Takai. 1993. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J. Cell Biol. 120:1187-1195.
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 16
    • 0033614371 scopus 로고    scopus 로고
    • Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filaments
    • Kosako, H., H. Goto, M. Yanagida, K. Matsuzawa, M. Fujita, Y. Tomono, T. Okigaki, H. Odai, K. Kaibuchi, and M. Inagaki. 1999. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments. Oncogene. 18:2783-2788.
    • (1999) Oncogene , vol.18 , pp. 2783-2788
    • Kosako, H.1    Goto, H.2    Yanagida, M.3    Matsuzawa, K.4    Fujita, M.5    Tomono, Y.6    Okigaki, T.7    Odai, H.8    Kaibuchi, K.9    Inagaki, M.10
  • 17
    • 0034619765 scopus 로고    scopus 로고
    • Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow
    • Kosako, H., T. Yoshida, F. Matsumura, T. Ishizaki, S. Narumiya, and M. Inagaki. 2000. Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene. 19:6059-6064.
    • (2000) Oncogene , vol.19 , pp. 6059-6064
    • Kosako, H.1    Yoshida, T.2    Matsumura, F.3    Ishizaki, T.4    Narumiya, S.5    Inagaki, M.6
  • 19
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi, I., Y. Hamaguchi, H. Fujimoto, N. Morii, M. Mishima, and S. Narumiya. 1993. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote. 1:325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 21
    • 0037455574 scopus 로고    scopus 로고
    • RhoA is required for cortical retraction and rigidity during mitotic cell rounding
    • Maddox, A.S., and K. Burridge. 2003. RhoA is required for cortical retraction and rigidity during mitotic cell rounding. J. Cell Biol. 160:255-265.
    • (2003) J. Cell Biol. , vol.160 , pp. 255-265
    • Maddox, A.S.1    Burridge, K.2
  • 22
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D., J. Silletti, G. Murphy, P. D'Eustachio, M. Rush, and M.R. Philips. 2001. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152:111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 23
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • Mitra, R.D., C.M. Silva, and D.C. Youvan. 1996. Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene. 173:13-17.
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 24
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer
    • Miyawaki, A., and R.Y. Tsien. 2000. Monitoring protein conformations and interactions by fluorescence resonance energy transfer. Methods Enzymol. 327:472-500.
    • (2000) Methods Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 26
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno, H., A. Sawano, P. Eli, H. Hama, and A. Miyawaki. 2001. Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry. 40:2502-2510.
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 28
    • 0035806898 scopus 로고    scopus 로고
    • Role of prenylation in the interaction of Rho-family small GTPases with GTPase activating proteins
    • Molnar, G., M.C. Dagher, M. Geiszt, J. Settleman, and E. Ligeti. 2001. Role of prenylation in the interaction of Rho-family small GTPases with GTPase activating proteins. Biochemistry. 40:10542-10549.
    • (2001) Biochemistry , vol.40 , pp. 10542-10549
    • Molnar, G.1    Dagher, M.C.2    Geiszt, M.3    Settleman, J.4    Ligeti, E.5
  • 29
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar, W.H. 1995. Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270:12949-12952.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 30
    • 0036024589 scopus 로고    scopus 로고
    • Constitutive active GTPases Rac and Cdc42 are associated with endoreplication in PAE cells
    • Muris, D., T. Verschoor, N. Divecha, and R. Michalides. 2002. Constitutive active GTPases Rac and Cdc42 are associated with endoreplication in PAE cells. Eur. J. Cancer. 38:1775-1782.
    • (2002) Eur. J. Cancer , vol.38 , pp. 1775-1782
    • Muris, D.1    Verschoor, T.2    Divecha, N.3    Michalides, R.4
  • 31
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., K. Ibata, E.S. Park, M. Kubota, K. Mikoshiba, and A. Miyawaki. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 32
    • 18744388826 scopus 로고    scopus 로고
    • Grit, a GTPase-activating protein for the Rho family, regulates neurite extension through its association with TrkA receptor and N-Shc, CrkL/Crk adapter molecules
    • Nakamura, T., M. Komiya, K. Sone, E. Hirose, N. Gotoh, H. Morii, Y. Ohta, and N. Mori. 2002. Grit, a GTPase-activating protein for the Rho family, regulates neurite extension through its association with TrkA receptor and N-Shc, CrkL/Crk adapter molecules. Mol. Cell. Biol. 22:8721-8734.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8721-8734
    • Nakamura, T.1    Komiya, M.2    Sone, K.3    Hirose, E.4    Gotoh, N.5    Morii, H.6    Ohta, Y.7    Mori, N.8
  • 33
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya, S. 1996. The small GTPase Rho: cellular functions and signal transduction. J. Biochem. (Tokyo). 120:215-228.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 34
    • 0031049976 scopus 로고    scopus 로고
    • Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: Redistribution of the nuclei, rearrangement of the actin system and formation of the cleavage furrow
    • Neujahr, R., C. Heizer, and G. Gerisch. 1997. Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, rearrangement of the actin system and formation of the cleavage furrow. J. Cell Sci. 110:123-137.
    • (1997) J. Cell Sci. , vol.110 , pp. 123-137
    • Neujahr, R.1    Heizer, C.2    Gerisch, G.3
  • 35
    • 0032423641 scopus 로고    scopus 로고
    • Localization of Rho GTPase in sea urchin eggs
    • Nishimura, Y., K. Nakano, and I. Mabuchi. 1998. Localization of Rho GTPase in sea urchin eggs. FEBS Lett. 441:121-126.
    • (1998) FEBS Lett. , vol.441 , pp. 121-126
    • Nishimura, Y.1    Nakano, K.2    Mabuchi, I.3
  • 36
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene. 108:193-200.
    • (1991) Gene , vol.108 , pp. 193-200
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 37
    • 0033601744 scopus 로고    scopus 로고
    • The small GTP-binding protein rho regulates cortical activities in cultured cells during division
    • O'Connell, C.B., S.P. Wheatley, S. Ahmed, and Y.L. Wang. 1999. The small GTP-binding protein rho regulates cortical activities in cultured cells during division. J. Cell Biol. 144:305-313.
    • (1999) J. Cell Biol. , vol.144 , pp. 305-313
    • O'Connell, C.B.1    Wheatley, S.P.2    Ahmed, S.3    Wang, Y.L.4
  • 38
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling
    • Olofsson, B. 1999. Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell. Signal. 11:545-554.
    • (1999) Cell. Signal. , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 39
    • 0034611015 scopus 로고    scopus 로고
    • Untying the Gordian knot of cytokinesis. Role of small G proteins and their regulators
    • Prokopenko, S.N., R. Saint, and H.J. Bellen. 2000. Untying the Gordian knot of cytokinesis. Role of small G proteins and their regulators. J. Cell Biol. 148:843-848.
    • (2000) J. Cell Biol. , vol.148 , pp. 843-848
    • Prokopenko, S.N.1    Saint, R.2    Bellen, H.J.3
  • 40
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L.C., F. Matsumura, G.M. Bokoch, and P. de Lanerolle. 1999. Inhibition of myosin light chain kinase by p21-activated kinase. Science. 283:2083-2085.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4
  • 41
    • 0024755672 scopus 로고
    • In pursuit of myosin function
    • Spudich, J.A. 1989. In pursuit of myosin function. Cell Regul. 1:1-11.
    • (1989) Cell Regul. , vol.1 , pp. 1-11
    • Spudich, J.A.1
  • 43
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi, K., T. Sasaki, T. Kameyama, S. Tsukita, S. Tsukita, 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.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 45
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui, Y., M. Amano, K. Nagata, N. Inagaki, H. Nakamura, H. Saya, K. Kaibuchi, and M. Inagaki. 1998. Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J. Cell Biol. 143:1249-1258.
    • (1998) J. Cell Biol. , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Nagata, K.3    Inagaki, N.4    Nakamura, H.5    Saya, H.6    Kaibuchi, K.7    Inagaki, M.8
  • 46
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., J.D. Violin, A.C. Newton, and R.Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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