Structural Basis of the Rho GTPase Signaling

Journal of Biochemistry

Volumn 134, Issue 3, 2003, Pages 327-331

  Hakoshima, Toshio ^a   Shimizu, Toshiyuki ^b   Maesaki, Ryoko ^a  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

Cdc42; GAP; GDI; GEF; Rac; RhoA

Indexed keywords

CELL PROTEIN; GUANOSINE TRIPHOSPHATASE; PROTEIN CDC42; RAC1 PROTEIN; RAC2 PROTEIN; REGULATOR PROTEIN; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

CELL FUNCTION; CELL ULTRASTRUCTURE; CELLULAR DISTRIBUTION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CYTOSKELETON; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; HUMAN; HYDROLYSIS; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE TRANSPORT; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SHORT SURVEY; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

GTPASE-ACTIVATING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; RHO GTP-BINDING PROTEINS; SIGNAL TRANSDUCTION;

EID: 0142026434     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvg149     Document Type: Short Survey

References (33)

1. Manneville, S.E. and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635
2. Vetter, I.R. and Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions. Science, 294, 1299-1304
3. Ihara, K., Muraguchi, S., Kato, M., Shimizu, T., Shirakawa, M., Kuroda, S., Kaibuchi, K., and Hakoshima, T. (1998) Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J. Biol. Chem. 273, 9656-9666
4. Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R.K., Somlyo, A.V., Somlyo, A.P., and Derewenda, Z.S. (1997) Crystal structure of RhoA-GDP and its functional implications. Nat. Struct. Biol. 4, 699-703
5. Rudolph, M.G., Wittinghofer, A., and Vetter, I.R. (1999) Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: Two different nucleotide states in one crystal. Protein Sci. 8, 778-787
6. 2+-free form of RHOA complexed with GDP: Implications for the GDP/GTP exchange mechanism. J. Biol. Chem. 275, 18311-18317
7. Kaibuchi, K., Kuroda, S., and Amano, M, (1999) Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68, 459-486
8. Maesaki, R., Ihara, K., Shimizu, T., Kuroda, S., Kaibuchi, K., and Hakoshima, T. (1999) The structural basis of Rho effector recognition revealed by the crystal structure of human RhoA complexed with the effector domain of PKN/PRK1. Mol. Cell 4, 793-803
9. Mott, H.R., Owen, D., Nietlispach, D., Lowe, P.N., Manser, E., Lim, L., and Laue, E.D. (1999) Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK. Nature 399, 384-388
10. Abdul-Manan, N., Aghazadeh, B., Liu, G.A., Majumdar, A., Ouerfelli, O., Siminovitch, K.A., and Rosen, M.K. (1999) Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein. Nature 399, 379-383
11. Garrard, S.M., Capaldo, C.T., Gao, L., Rosen, M.K., Macara, I.G., and Tomchick, D.R. (2003) Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J. 22, 1125-1133
12. Morreale, A., Venkatesan, M., Mott, H.R., Owen, D., Nietlispach, D., Lowe, P.N., and Laue, E.D. (2000) Structure of Cdc42 bound to the GTPase binding domain of PAK. Nat. Struct. Biol. 7, 384-388
13. phox in complex with Rac-GTP. Mol. Cell 6, 899-907
14. Flynn, P., Meller, H., Palmer, R., Panayotou, G., and Parker, P.J. (1998) Multiple interactions of PRK1 with RhoA. J. Biol. Chem. 273, 2698-2705
15. Zong, H., Raman, N., Mickelson-Young, L.A., Atkinson, S.J., and Quilliam, L.A. (1999) Loop 6 of RhoA confers specificity for effector binding, stress fiber formation, and cellular transformation. J. Biol. Chem. 274, 4551-4560
16. Ostermeier, C. and Brunger, A.T. (1999) Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96, 363-374
17. Tarricone, C., Xiao, B., Justin, N., Walker, P.A., Rittinger, K., Gamblin, S.J., and Smerdon, S.J. (2001) The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 411, 215-219
18. Zheng, Y. (2001) Dbl family guanine nucleotide exchange factors. Trends Biochem. Sci. 26, 724-732
19. Schmidt, A. and Hall, A. (2002) Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16, 1587-1609
20. Worthylake, D.K., Rossman, K.L., and Sondek, J. (2000) Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 408, 682-688
21. Rossman, K.L., Worthylake, D.K., Snyder, J.T., Siderovski, D.P., Campbell, S.L., and Sondek, J. (2002) A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. EMBO J. 21, 1315-1326
22. Snyder, J.T., Worthylake, D.K., Rossman, K.L., Betts, L., Pruitt, W.M., Siderovski, D.P., Der, C.J., and Sondek, J. (2002) Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat. Struct. Biol. 9, 468-475
23. Rittinger, K., Walker, P.A., Eccleston, J.F., Nurmahomed, K., Owen, D., Laue, E., Gamblin, S.J., and Smerdon, S.J. (1997) Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature 388, 693-697
24. Rittinger, K., Walker, P.A., Eccleston, J.F., Smerdon, S.J., and Gamblin, S.J. (1997) Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762
25. Nassar, N., Hoffman, G.R., Manor, D., Clardy, J.C., and Cerione, R.A. (1998) Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat. Struct. Biol. 5, 1047-1052
26. Hoffman, G.R., Nassar, N., and Cerione, R.A. (2000) Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell 100, 345-356
27. Scheffzek, K., Stephan, I., Jensen, O.N., Illenberger, D., and Gierschik, P. (2000) The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat. Struct. Biol. 7, 122-126
28. Grizot, S., Fauré, J., Fieschi, F., Vignais, P.V., Dagher, M.C., and Peyroula, E.P. (2001) Crystal structure of the Rac1-RhoGDI complex involved in NADPH oxidase activation. Biochemistry 40, 10007-10013
29. Platko, J.V., Leonard, D.A., Adra, C.N., Shaw, R.J., Cerione, R.A., and Lim, B. (1995) A single residue can modify target-binding affinity and activity of the functional domain of the Rho-subfamily GDP dissociation inhibitors. Proc. Natl Acad. Sci. USA 92, 2974-2978
30. Schalk, I., Zeng, K., Wu, S.K., Stura, E.A., Matteson, J., Huang, M., Tandon, A., Wilson, I.A., and Balch, W.E. (1996) Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 381, 42-48
31. Hirshberg, M., Stockley, R.W., Dodson, G., and Webb, M.R. (1997) The crystal structure of human rac1, a member of the Rho-family complexed with a GTP analogue. Nat. Struct. Biol. 4, 147-152
32. Kraulis, P.J. (1991) MOLSCRIPT-A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950
33. Merritt, E.A. and Murphy, M.E.P. (1994) Raster3D ver. 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873