Functions and functional domains of the GTPase Cdc42p

Molecular Biology of the Cell

Volumn 11, Issue 1, 2000, Pages 339-354

  Kozminski, Keith G ^a   Chen, Ann J ^a   Rodal, Avital A ^a   Drubin, David G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE;

ARTICLE; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME STRUCTURE; GENE MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS;

EUKARYOTA; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES;

EID: 0033965023     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.1.339     Document Type: Article

References (79)

1. 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.
2. Adams, A.E., Johnson, D.I., Longnecker, R.M., Sloat, B.F., and Pringle, J.R. (1990). CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 111, 131-142.
3. Adams, A.E., and Pringle, J.R. (1984). Relationship of actin and tubulin distribution to bud growth in wild-type and morphogenetic-mutant Saccharomyces cerevisiae. J. Cell Biol. 98, 934-945.
4. Adari, H., Lowy, D.R., Willumsen, B.M., Der, C.J., and McCormick, F. (1988). Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science 240, 518-521.
5. Aguilera, A. (1994). Formamide sensitivity: a novel conditional phenotype in yeast. Genetics 136, 87-91.
6. Altman, R., and Kellogg, D. (1997). Control of mitotic events by Nap1 and the Gin4 kinase. J. Cell Biol. 138, 119-130.
7. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., and Struhl, K. (1994). Current Protocols in Molecular Biology, New York: John Wiley & Sons.
8. Ayscough, K.R., and Drubin, D.G. (1998). Immunofluorescence microscopy of yeast cells. In: Cell Biology: A Laboratory Handbook, vol. 2, ed. J. Cells, New York: Academic Press, 447-485.
9. Belmont, L.D., and Drubin, D.G. (1998). The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 142, 1289-1299.
10. Boeke, J.D., LaCroute, F., and Fink, G.R. (1984). A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197, 345-346.
11. Bond, J.F., Fridovich-Keil, J.L., Pillus, L., Mulligan, R.C., and Solomon, F. (1986). A chicken-yeast chimeric β-tubulin protein is incorporated into mouse microtubules in vivo. Cell 44, 461-468.
12. Bourne, H.R., Sanders, D.A., and McCormick, F. (1991). The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127.
13. Brennwald, P., and Novick, P. (1993). Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362, 560-563.
14. Brown, J.L., Jaquenoud, M., Gulli, M.P., Chant, J., and Peter, M. (1997). Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast. Genes Dev. 11, 2972-2982.
15. Burbelo, P.D., Drechsel, D., and Hall, A. (1995). A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074.
16. Cabib, E., Drgonová, J., and Drgon, T. (1998). Role of small G proteins in yeast cell polarization and wall biosynthesis. Annu. Rev. Biochem. 67, 307-333.
17. Calés, C., Hancock, J.F., Marshall, C.J., and Hall, A. (1988). The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene product. Nature 332, 548-551.
18. Campbell, S.L., Khosravi-Far, R., Rossman, K.L., Clark, G.J., and Der, C.J. (1998). Increasing complexity of Ras signaling. Oncogene 17, 1395-1413.
19. Chen, G.C., Kim, Y.J., and Chan, C.S. (1997). The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae. Genes Dev. 11, 2958-2971.
20. Chothia, C. (1976). The nature of the accessible and buried surfaces in proteins. J. Mol. Biol. 105, 1-12.
21. Cvrcková, F., De Virgilio, C., Manser, E., Pringle, J.R., and Nasmyth, K. (1995). Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Genes Dev. 9, 1817-1830.
22. Davis, C.R., Richman, T.J., Deliduka, S.B., Blaisdell, J.O., Collins, C.C., and Johnson, D.I. (1998). Analysis of the mechanisms of action of the Saccharomyces cerevisiae dominant lethal cdc42G12V and dominant negative cdc42D118A mutations. J. Biol. Chem. 273, 849-858.
23. Dunn, B., Stearns, T., and Botstein, D. (1993). Specificity domains distinguish the Ras-related GTPases Ypt1 and Sec4. Nature 362, 563-565.
24. Eby, J.J., Holly, S.P., van Drogen, F., Grishin, A.V., Peter, M., Drubin, D.G., and Blumer, K.J. (1998). Actin cytoskeleton organization regulated by the PAK family of protein kinases. Curr. Biol. 8, 967-970.
25. Feltham, J.L., Dötsch, V., Raza, S., Manor, D., Cerione, R.A., Sutcliffe, M.J., Wagner, G., and Oswald, R.E. (1997). Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry 36, 8755-8766.
26. Freeman, J.L., Abo, A., and Lambeth, J.D. (1996). Rac "insert region" is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J. Biol. Chem. 271, 19794-19801.
27. Garcia-Ranea, J.A., and Valencia, A. (1998). Distribution and functional diversification of the ras superfamily in Saccharomyces cerevisiae. FEBS Lett. 434, 219-225.
28. Guo, W., Sutcliffe, M.J., Cerione, R.A., and Oswald, R.E. (1998). Identification of the binding surface on Cdc42Hs for p21-activated kinase. Biochemistry 37, 14030-14037.
29. Hoffman, G.R., Nassar, N., Oswald, R.E., and Cerione, R.A. (1998). Fluoride activation of the Rho family GTP-binding protein Cdc42Hs. J. Biol. Chem. 273, 4392-4399.
30. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
31. Johnson, D.I. (1999). Cdc42: an essential Rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63, 54-105.
32. Johnson, D.I., and Pringle, J.R. (1990). Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111, 143-152.
33. Johnston, M., and Davis, R.W. (1984). Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae. Mol. Cell. Biol. 4, 1440-1448.
34. Joneson, T., and Bar-Sagi, D. (1998). A Rac1 effector site controlling mitogenesis through superoxide production. J. Biol. Chem, 273, 17991-17994.
35. Joseph, G., and Pick, E. (1995). "Peptide walking" is a novel method for mapping functional domains in proteins: its application to the Rac1-dependent activation of NADPH oxidase. J. Biol. Chem. 270, 29079-29082.
36. Kozminski, K.G., Diener, D.R., and Rosenbaum, J.L. (1993). High level expression of nonacetylatable α-tubulin in Chlamydomonas reinhardtii. Cell Motil. Cytoskeleton 25, 158-170.
37. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
38. PAK and the JNK/SAPK MAP kinase cascade. Cell 87, 519-529.
39. Lappalainen, P., Fedorov, E.V., Fedorov, A.A., Almo, S.C., and Drubin, D.G. (1997). Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 16, 5520-5530.
40. Leberer, E., Wu, C., Leeuw, T., Fourest-Lieuvin, A., Segall, J.E., and Thomas, D.Y. (1997). Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase. EMBO J. 16, 83-97.
41. Li, R., and Zheng, Y. (1997). Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Db1-like guanine nucleotide exchange factors. J. Biol. Chem. 272, 4671-4679.
42. Mackay, D.J., and Hall, A. (1998). Rho GTPases. J. Biol. Chem. 273, 20685-20688.
43. Madden, K., and Snyder, M. (1998). Cell polarity and morphogenesis in budding yeast. Annu. Rev. Microbiol. 52, 687-744.
44. Martín, H., Mendoza, A., Rodríguez-Pachón, J.M., Molina, M., and Nombela, C. (1997). Characterization of SKM1, a Saccharomyces cerevisiae gene encoding a novel Ste20/PAK-like protein kinase. Mol. Microbiol. 23, 431-444.
45. McCallum, S.J., Wu, W.J., and Cerione, R.A. (1996). Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAP1 and a Cdc42Hs binding partner with similarity to IQGAP2. J. Biol. Chem. 271, 21732-21737.
46. Miller, P.J., and Johnson, D.I. (1994). Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe. Mol. Cell. Biol. 14, 1075-1083.
47. ts allele and new temperature-conditional-lethal cdc42 alleles. Yeast 13, 561-572.
48. 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.
49. Mulholland, J., Preuss, D., Moon, A., Wong, A., Drubin, D., and Botstein, D. (1994). Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125, 381-391.
50. Munemitsu, S., Innis, M.A., Clark, R., McCormick, F., Ullrich, A., and Polakis, P. (1990). Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol. Cell. Biol. 10, 5977-5982.
51. 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.
52. Nonaka, H., Tanaka, K., Hirano, H., Fujiwara, T., Kohno, H., Umikawa, M., Mino, A., and Takai, Y. (1995). A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J. 14, 5931-5938.
53. Ohya, Y., Qadota, H., Anraku, Y., Pringle, J.R., and Botstein, D. (1993). Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rholp and Cdc42p. Mol. Biol. Cell 4, 1017-1025.
54. Peränen, J., Rikkonen, M., Hyvönen, M., and Kääriäinen, L. (1996). T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236, 371-373.
55. Peter, M., Neiman, A.M., Park, H.O., van Lohuizen, M., and Herskowitz, I. (1996). Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. EMBO J. 15, 7046-7059.
56. 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.
57. Sahai, E., Alberts, A.S., and Treisman, R. (1998). RhoA effector mutants reveal distinct effector pathways for cytoskeletal reorganization, SRF activation and transformation. EMBO J. 17, 1350-1361.
58. Schiestl, R.H., and Gietz, R.D. (1989). High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16, 339-346.
59. Schmidt, A., and Hall, M.N. (1998). Signaling to the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 14, 305-338.
60. Self, A.J., Paterson, H.F., and Hall, A. (1993). Different structural organization of Ras and Rho effector domains. Oncogene 8, 655-661.
61. Sherman, F., Fink, G.R., and Hicks, J.B. (1986). Methods in Yeast Genetics, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
62. Shinjo, K., Koland, J.G., Hart, M.J., Narasimhan, V., Johnson, D.I., Evans, T., and Cerione, R.A. (1990). Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc. Natl. Acad. Sci. USA 87, 9853-9857.
63. Sigal, I.S., Gibbs, J.B., D'Alonzo, J.S., and Scolnick, E.M. (1986). Identification of effector residues and a neutralizing epitope of Ha-ras-encoded p21. Proc. Natl. Acad. Sci. USA 83, 4725-4729.
64. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
65. Stenmark, H., Valencia, A., Martinez, O., Ullrich, O., Goud, B., and Zerial, M. (1994). Distinct structural elements of rab5 define its functional specificity. EMBO J. 13, 575-583.
66. Stevens, W.K., Vranken, W., Goudreau, N., Xiang, H., Xu, P., and Ni, F. (1999). Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. Biochemistry 38, 5968-5975.
67. Stowers, L., Yelon, D., Berg, L.J., and Chant, J. (1995). Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc. Natl. Acad. Sci. USA 92, 5027-5031.
68. Tjandra, H., Compton, J., and Kellogg, D. (1998). Control of mitotic events by the Cdc42 GTPase, the Clb2 cyclin and a member of the PAK kinase family. Curr. Biol. 8, 991-1000.
69. Valencia, A., Chardin, P., Wittinghofer, A., and Sander, C. (1991). The ras protein family: evolutionary tree and role of conserved amino acids. Biochemistry 30, 4637-4648.
70. 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.
71. Wertman, K.F., Drubin, D.G., and Botstein, D. (1992). Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350.
72. Wu, W.J., Lin, R., Cerione, R.A., and Manor, D. (1998). Transformation activity of Cdc42 requires a region unique to Rho-related proteins. J. Biol. Chem. 273, 16655-16658.
73. Xu, X., Barry, D.C., Settleman, J., Schwartz, M.A., and Bokoch, G.M. (1994). Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac. J. Biol. Chem. 269, 23569-23574.
74. Zerial, M., and Huber, L.A. (1995). Guidebook to the Small GTPases, New York: Sambrook and Tooze.
75. Zheng, Y., Cerione, R., and Bender, A. (1994). Control of the yeast bud-site assembly GTPase Cdc42: catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J. Biol. Chem. 269, 2369-2372.
76. Ziman, M., O'Brien, J.M., Ouellette, L.A., Church, W.R., and Johnson, D.I. (1991). Mutational analysis of CDC42Sc, a Scccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol. Cell. Biol. 11, 3537-3544.
77. Ziman, M., Preuss, D., Mulholland, J., O'Brien, J.M., Botstein, D., and Johnson, D.I. (1993). Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell 4, 1307-1316.
78. Zohar, M., Teramoto, H., Katz, B.Z., Yamada, K.M., and Gutkind, J.S. (1998). Effector domain mutants of Rho dissociate cytoskeletal changes from nuclear signaling and cellular transformation. Oncogene 17, 991-998.
79. Zohn, I.M., Campbell, S.L., Khosravi-Far, R., Rossman, K.L., and Der, C.J. (1998). Rho family proteins and Ras transformation: the RHOad less traveled gets congested. Oncogene 17, 1415-1438.