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Volumn 262, Issue 3, 1999, Pages 879-889

Phosphoinositide-dependent activation of Rho A involves partial opening of the RhoA/Rho-GDI complex

Author keywords

ADP ribosylation; Phosphoinositides; Prenylation; Rho GTPases; Rho GDI

Indexed keywords

GLUTATHIONE TRANSFERASE; GUANOSINE TRIPHOSPHATASE; HYBRID PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHATIDYLINOSITIDE;

EID: 0001678613     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00458.x     Document Type: Article
Times cited : (57)

References (41)
  • 2
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • 2. Vojtek, A.B. & Cooper, J.A. (1995) Rho family members: activators of MAP kinase cascades. Cell 82, 527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 3
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • 3. Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 4
    • 0031046030 scopus 로고    scopus 로고
    • Rho GTPases and leukocyte cytoskeletal regulation
    • 4. Dharmawardhane, S. & Bokoch, G.M. (1997) Rho GTPases and leukocyte cytoskeletal regulation. Curr. Opin. Hematology 4, 12-18.
    • (1997) Curr. Opin. Hematology , vol.4 , pp. 12-18
    • Dharmawardhane, S.1    Bokoch, G.M.2
  • 5
    • 0025906597 scopus 로고
    • Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins
    • 5. Hori, Y., Kikuchi, A., Isomura, M., Katayama, M., Miura, Y., Fujioka, H., Kaibuchi, K. & Takai, Y. (1991) Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 6, 515-522.
    • (1991) Oncogene , vol.6 , pp. 515-522
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 6
    • 0025295180 scopus 로고
    • Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of gdp from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein
    • 6. Ueda, T., Kikuchi, A., Ohga, N., Yamamoto, J. & Takai, Y. (1990) Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein. J. Biol. Chem. 265, 9373-9380.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9373-9380
    • Ueda, T.1    Kikuchi, A.2    Ohga, N.3    Yamamoto, J.4    Takai, Y.5
  • 7
    • 0030992879 scopus 로고    scopus 로고
    • C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases
    • 7. Gosser, Y.Q., Nomanbhoy, T.K., Aghazadeh, B., Manor, D., Combs, C., Cerione, R.A. & Rosen, M.K. (1997) C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature 387, 814-819.
    • (1997) Nature , vol.387 , pp. 814-819
    • Gosser, Y.Q.1    Nomanbhoy, T.K.2    Aghazadeh, B.3    Manor, D.4    Combs, C.5    Cerione, R.A.6    Rosen, M.K.7
  • 8
    • 0031570337 scopus 로고    scopus 로고
    • A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    • 8. Keep, N.H., Barnes, M., Barsukow, I., Badii, R., Lian, L.-Y., Segal, A.W., Moody, P.C.E. & Roberts, G.C.K. (1997) A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633.
    • (1997) Structure , vol.5 , pp. 623-633
    • Keep, N.H.1    Barnes, M.2    Barsukow, I.3    Badii, R.4    Lian, L.-Y.5    Segal, A.W.6    Moody, P.C.E.7    Roberts, G.C.K.8
  • 9
    • 0032576997 scopus 로고    scopus 로고
    • The Rho small G protein family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control
    • 9. Sasaki, T. & Takai, Y. (1998) The Rho small G protein family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control. Biochem. Biophys. Res. Commun. 245, 641-645.
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 641-645
    • Sasaki, T.1    Takai, Y.2
  • 10
    • 0027526303 scopus 로고
    • cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the Rho GTP-binding proteins
    • 10. Lelias, J.-M., Adra, C.N., Gerburg, M.W., Guillemot, J.-C., Khagad, M., Caput, D. & Lim, B. (1993) cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the Rho GTP-binding proteins. Proc. Natl Acad. Sci. USA 90, 1479-1483.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1479-1483
    • Lelias, J.-M.1    Adra, C.N.2    Gerburg, M.W.3    Guillemot, J.-C.4    Khagad, M.5    Caput, D.6    Lim, B.7
  • 11
    • 0027237511 scopus 로고
    • Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes
    • 11. Scherle, P., Behrens, T. & Staudt, L.M. (1993) Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes. Proc. Natl Acad. Sci. USA 90, 7568-7572.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7568-7572
    • Scherle, P.1    Behrens, T.2    Staudt, L.M.3
  • 12
    • 0032579315 scopus 로고    scopus 로고
    • Differential properties of D4/LyGDI versus RhoGDI: Phosphorylation and rho GTPase selectivity
    • 12. Gorvel, J.-P., Chang, T.-C., Boretto, J., Azuma, T. & Chavrier, P. (1998) Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity. FEBS Lett. 422, 269-273.
    • (1998) FEBS Lett. , vol.422 , pp. 269-273
    • Gorvel, J.-P.1    Chang, T.-C.2    Boretto, J.3    Azuma, T.4    Chavrier, P.5
  • 14
    • 0030611196 scopus 로고    scopus 로고
    • RhoGDIgamma: A GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas
    • 14. Adra, C.N., Manor, D., Ko, J.L., Zhu, S., Horiuchi, T., Van Aelst, L., Cerione, R.A. & Lim, B. (1997) RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proc. Natl Acad. Sci. USA 94, 4279-4284.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4279-4284
    • Adra, C.N.1    Manor, D.2    Ko, J.L.3    Zhu, S.4    Horiuchi, T.5    Van Aelst, L.6    Cerione, R.A.7    Lim, B.8
  • 15
    • 0025833804 scopus 로고
    • ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility
    • 15. Stasia, M.J., Jouan, A., Bourmeyster, N., Boquet, P. & Vignais, P.V. (1991) ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility. Biochem. Biophys. Res. Commun 180, 615-622.
    • (1991) Biochem. Biophys. Res. Commun , vol.180 , pp. 615-622
    • Stasia, M.J.1    Jouan, A.2    Bourmeyster, N.3    Boquet, P.4    Vignais, P.V.5
  • 17
    • 0002264813 scopus 로고
    • Abramson, J.S. & Wheeler, J.C., eds. IRL Press, Oxford
    • 17. McPhail, L.C. & Harvath, L. (1993) In the Natural Immune System (Abramson, J.S. & Wheeler, J.C., eds), pp. 63-107. IRL Press, Oxford.
    • (1993) The Natural Immune System , pp. 63-107
    • McPhail, L.C.1    Harvath, L.2
  • 18
    • 0030684003 scopus 로고    scopus 로고
    • Requirement for both rac1 and Cdc42 in membrane ruffling and phagocytosis in leukocytes
    • 18. Cox, D., Chang, P., Zhang, Q., Copal Reddy, P., Bokoch, G.M. & Greenberg, S. (1997) Requirement for both rac1 and Cdc42 in membrane ruffling and phagocytosis in leukocytes. J. Exp Med. 186, 1487-1494.
    • (1997) J. Exp Med. , vol.186 , pp. 1487-1494
    • Cox, D.1    Chang, P.2    Zhang, Q.3    Copal Reddy, P.4    Bokoch, G.M.5    Greenberg, S.6
  • 19
    • 0027102910 scopus 로고
    • Copurification of rho protein and the rho-GDP dissociation inhibitor from bovine neutrophil cytosol. Effect of phosphoinositides on rho ADP-ribosylation by the C3 exoenzyme of Clostridium botulinum
    • 19. Bourmeyster, N., Stasia, M.J., Garin, J., Gagnon, J., Boquet, P. & Vignais, P.V. (1992) Copurification of rho protein and the rho-GDP dissociation inhibitor from bovine neutrophil cytosol. Effect of phosphoinositides on rho ADP-ribosylation by the C3 exoenzyme of Clostridium botulinum. Biochemistry 31, 12863-12869.
    • (1992) Biochemistry , vol.31 , pp. 12863-12869
    • Bourmeyster, N.1    Stasia, M.J.2    Garin, J.3    Gagnon, J.4    Boquet, P.5    Vignais, P.V.6
  • 20
    • 0027442667 scopus 로고
    • Biologically active lipids are regulators of Rac. GDI complexation
    • 20. Chuang, T.-H., Bohl, B.P. & Bokoch, G.M. (1993) Biologically active lipids are regulators of Rac. GDI complexation. J. Biol. Chem. 268, 26206-26211.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26206-26211
    • Chuang, T.-H.1    Bohl, B.P.2    Bokoch, G.M.3
  • 21
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • 21. Sekine, A., Fujiwara, M. & Narumiya, S. (1989) Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem 264, 8602-8605.
    • (1989) J. Biol. Chem , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 22
    • 0000278553 scopus 로고    scopus 로고
    • Intracellular signals and the cytoskeleton: The interactions of phosphoinositide kinases and small G proteins in adherence, ruffling and motility
    • 22. Carpenter, C.L. (1996) Intracellular signals and the cytoskeleton: the interactions of phosphoinositide kinases and small G proteins in adherence, ruffling and motility. Seminars Cell Dev. Biol. 7, 691-697.
    • (1996) Seminars Cell Dev. Biol. , vol.7 , pp. 691-697
    • Carpenter, C.L.1
  • 23
    • 0027464867 scopus 로고
    • Polyvinylpyrrolidone as a blocking agent in immunochemical studies
    • 23. Haycock, J.W. (1993) Polyvinylpyrrolidone as a blocking agent in immunochemical studies. Anal. Biochem. 208, 397-399.
    • (1993) Anal. Biochem. , vol.208 , pp. 397-399
    • Haycock, J.W.1
  • 24
    • 0028916743 scopus 로고
    • Photoaffinity labeling and photoinactivation of the O2-generating oxidase of neutrophils by an azido derivative of FAD
    • 24. Doussiere, J., Buzenet, G. & Vignais, P.V. (1995) Photoaffinity labeling and photoinactivation of the O2-generating oxidase of neutrophils by an azido derivative of FAD. Biochemistry 34, 1760-1770.
    • (1995) Biochemistry , vol.34 , pp. 1760-1770
    • Doussiere, J.1    Buzenet, G.2    Vignais, P.V.3
  • 25
  • 26
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • 26. Bokoch, G.M., Bohl, B.P. & Chuang, T.-H. (1994) Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem 269, 31674-31679.
    • (1994) J. Biol. Chem , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.-H.3
  • 27
    • 0032521556 scopus 로고    scopus 로고
    • Guanine nucleotide-dependent translocation of RhoA from cytosol to high affinity membrane binding sites in human erythrocytes
    • 27. Boukharov, A.A. & Cohen, C.M. (1998) Guanine nucleotide-dependent translocation of RhoA from cytosol to high affinity membrane binding sites in human erythrocytes. Biochem. J. 330, 1391-1398.
    • (1998) Biochem. J. , vol.330 , pp. 1391-1398
    • Boukharov, A.A.1    Cohen, C.M.2
  • 28
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • 28. Rittinger, K., Walker, P.A., Eccleston, J.F., Smerdon, S.J. & Gamblin, S.J. (1997) Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 29
    • 0026664194 scopus 로고
    • Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein
    • 29. Kikuchi, A., Kuroda, S., Sasaki, T., Kotani, K., Hirata, K., Katayama, M. & Takai, Y. (1992) Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein. J. Biol. Chem 267, 14611-14615.
    • (1992) J. Biol. Chem , vol.267 , pp. 14611-14615
    • Kikuchi, A.1    Kuroda, S.2    Sasaki, T.3    Kotani, K.4    Hirata, K.5    Katayama, M.6    Takai, Y.7
  • 30
    • 0028239341 scopus 로고
    • The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: Its properties in comparison with those of Smg GDS
    • 30. Yaku, H., Sasaki, T. & Takai, Y. (1994) The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: its properties in comparison with those of Smg GDS. Biochem. Biophys. Res. Commun 198, 811-817.
    • (1994) Biochem. Biophys. Res. Commun , vol.198 , pp. 811-817
    • Yaku, H.1    Sasaki, T.2    Takai, Y.3
  • 31
    • 0024457508 scopus 로고
    • From signal to pseudopod. How cells control cytoplasmic actin assembly
    • 31. Stossel, T.P. (1989) From signal to pseudopod. How cells control cytoplasmic actin assembly. J. Biol. Chem 264, 18261-18264.
    • (1989) J. Biol. Chem , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 32
  • 33
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • 33. Zheng, Y., Bagrodia, S. & Cerione, R.A. (1994) Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem 269, 18727-18730.
    • (1994) J. Biol. Chem , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 34
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • 34. Tolias, K.F., Cantley, L.C. & Carpenter, C.L. (1995) Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem 270, 17656-17659.
    • (1995) J. Biol. Chem , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 35
    • 0025611910 scopus 로고
    • Phosphoinositides kinases
    • 35. Carpenter, C.L. & Cantley, L.C. (1990) Phosphoinositides kinases. Biochemistry 29, 11147-11156.
    • (1990) Biochemistry , vol.29 , pp. 11147-11156
    • Carpenter, C.L.1    Cantley, L.C.2
  • 36
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho
    • 36. Zhang, J., King, W.G., Dillon, S., Hall, A., Feig, L. & Rittenhouse, S.E. (1993) Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein Rho. J. Biol. Chem 268, 22251-22254.
    • (1993) J. Biol. Chem , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.G.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.E.6
  • 37
    • 0031882760 scopus 로고    scopus 로고
    • Characterization of a Racl- and RhoGDI-associated lipid kinase signaling complex
    • 37. Tolias, K.F., Couvillon, A.D., Cantley, L.C. & Carpenter, C.L. (1998) Characterization of a Racl- and RhoGDI-associated lipid kinase signaling complex. Mol Cell Biol. 18, 762-770.
    • (1998) Mol Cell Biol. , vol.18 , pp. 762-770
    • Tolias, K.F.1    Couvillon, A.D.2    Cantley, L.C.3    Carpenter, C.L.4
  • 38
    • 0029835783 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs
    • 38. Zheng, Y., Glaven, J.A., Wu, W.J. & Cerione, R.A. (1996) Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs. J. Biol. Chem 271, 23815-23819.
    • (1996) J. Biol. Chem , vol.271 , pp. 23815-23819
    • Zheng, Y.1    Glaven, J.A.2    Wu, W.J.3    Cerione, R.A.4
  • 39
    • 0032514903 scopus 로고    scopus 로고
    • Lipid products of phosphoinositide 3-kinase interact with rac1 GTPase and stimulate GDP dissociation
    • 39. Missy, K., Van Poucke, V., Raynal, P., Viala, C., Mauco, G., Plantavid, M., Chap, H. & Payrastre, B. (1998) Lipid products of phosphoinositide 3-kinase interact with rac1 GTPase and stimulate GDP dissociation. J. Biol. Chem 273, 30279-30286.
    • (1998) J. Biol. Chem , vol.273 , pp. 30279-30286
    • Missy, K.1    Van Poucke, V.2    Raynal, P.3    Viala, C.4    Mauco, G.5    Plantavid, M.6    Chap, H.7    Payrastre, B.8
  • 40
    • 0031023505 scopus 로고    scopus 로고
    • Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI
    • 40. Dirac-Svejstrup, A.B., Sumizawa, T. & Pfeffer, S.R. (1997) Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J. 16, 366-472.
    • (1997) EMBO J. , vol.16 , pp. 366-472
    • Dirac-Svejstrup, A.B.1    Sumizawa, T.2    Pfeffer, S.R.3
  • 41
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with Ezrin/Radixin/Moesin initiates the activation of the Rho small G protein
    • 41. Takahashi, K., Sasaki, T., Mammoto, A., Takaishi, K., Kameyama, T., Tsukita, S., Tsukita, S. & Takai, Y. (1997) Direct interaction of the Rho GDP dissociation inhibitor with Ezrin/Radixin/Moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272, 23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Tsukita, S.7    Takai, Y.8


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