The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity

FEBS Letters

Volumn 579, Issue 30, 2005, Pages 6851-6858

  Sacco, Elena ^a   Fantinato, Sonia ^a   Manzoni, Romilde ^a   Metalli, David ^a   De Gioia, Luca ^a   Fantucci, Piercarlo ^a   Alberghina, Lilia ^a   Vanoni, Marco ^a  

^a UNIVERSITY OF MILANO BICOCCA   (Italy)

Author keywords

Cdc25Mm; Dominant negative mutants; Guanine nucleotide exchange factor; HI hairpin; Ras inhibitor

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; NUCLEOTIDE; PROTEIN CDC25 MM; PROTEIN INHIBITOR; RAS PROTEIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CATALYSIS; CELL STRAIN 3T3; COMPLEX FORMATION; CONTROLLED STUDY; DISSOCIATION; DOWN REGULATION; GENE MUTATION; MOLECULAR MODEL; MOUSE; NONHUMAN; NUCLEOTIDE METABOLISM; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; ANTHRANILIC ACIDS; BUFFERS; CATALYSIS; CATALYTIC DOMAIN; CELL LINE, TRANSFORMED; CELL TRANSFORMATION, NEOPLASTIC; CRYSTALLOGRAPHY, X-RAY; DOWN-REGULATION; ESCHERICHIA COLI; FIBROBLASTS; GENES, DOMINANT; GENES, RAS; GENES, REPORTER; GLUTAMIC ACID; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HOMOZYGOTE; LUCIFERASES; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NIH 3T3 CELLS; PROTEIN STRUCTURE, SECONDARY; RAS-GRF1; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

ANIMALIA; MAMMALIA;

EID: 28844438376     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.11.024     Document Type: Article

References (36)

1. S.R. Hingorani, and D.A. Tuveson Ras redux: rethinking how and where Ras acts Curr. Opin. Genet. Dev. 13 2003 6 13
2. F. Wittinghofer Ras signalling. Caught in the act of the switch-on Nature 394 1998 317 319-320
3. I.R. Vetter, and A. Wittinghofer The guanine nucleotide-binding switch in three dimensions Science 294 2001 1299 1304
4. M.S. Boguski, and F. McCormick Proteins regulating Ras and its relatives Nature 366 1993 643 654
5. D.R. Lowy, M.R. Johnson, J.E. DeClue, H. Cen, K. Zhang, A.G. Papageorge, W.C. Vass, B.M. Willumsen, M.B. Valentine, and A.T. Look Cell transformation by ras and regulation of its protein product Ciba Found. Symp. 176 1993 67 80 discussion 80-4
6. L.A. Quilliam, J.F. Rebhun, and A.F. Castro A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases Prog. Nucleic Acid Res. Mol. Biol. 71 2002 391 444
7. G.M. Springett, H. Kawasaki, and D.R. Spriggs Non-kinase second-messenger signaling: new pathways with new promise Bioessays 26 2004 730 738
8. P.A. Boriack-Sjodin, S.M. Margarit, D. Bar-Sagi, and J. Kuriyan The structural basis of the activation of Ras by Sos Nature 394 1998 337 343
9. H. Sondermann, S.M. Soisson, S. Boykevisch, S.S. Yang, D. Bar-Sagi, and J. Kuriyan Structural analysis of autoinhibition in the Ras activator Son of sevenless Cell 119 2004 393 405
10. S. Baouz, E. Jacquet, K. Accorsi, C. Hountondji, M. Balestrini, R. Zippel, E. Sturani, and A. Parmeggiani Sites of phosphorylation by protein kinase A in CDC25Mm/GRF1, a guanine nucleotide exchange factor for Ras J. Biol. Chem. 276 2001 1742 1749
11. B.E. Hall, S.S. Yang, P.A. Boriack-Sjodin, J. Kuriyan, and D. Bar-Sagi Structure-based mutagenesis reveals distinct functions for Ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange J. Biol. Chem. 276 2001 27629 27637
12. S.M. Margarit, H. Sondermann, B.E. Hall, B. Nagar, A. Hoelz, M. Pirruccello, D. Bar-Sagi, and J. Kuriyan Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS Cell 112 2003 685 695
13. M. Vanoni, R. Bertini, E. Sacco, L. Fontanella, M. Rieppi, S. Colombo, E. Martegani, V. Carrera, A. Moroni, C. Bizzarri, V. Sabbatini, M. Cattozzo, A. Colagrande, and L. Alberghina Characterization and properties of dominant-negative mutants of the ras-specific guanine nucleotide exchange factor CDC25(Mm) J. Biol. Chem. 274 1999 36656 36662
14. V. Carrera, A. Moroni, E. Martegani, C. Volponi, R.H. Cool, L. Alberghina, and M. Vanoni Mutations at position 1122 in the catalytic domain of the mouse ras-specific guanine nucleotide exchange factor CDC25Mm originate both loss-of-function and gain-of-function proteins FEBS Lett. 440 1998 291 296
15. W. Park, R.D. Mosteller, and D. Broek Amino acid residues in the CDC25 guanine nucleotide exchange factor critical for interaction with Ras Mol. Cell. Biol. 14 1994 8117 8122
16. C. Lenzen, R.H. Cool, H. Prinz, J. Kuhlmann, and A. Wittinghofer Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm Biochemistry 37 1998 7420 7430
17. B. Zhang, Y. Zhang, E. Shacter, and Y. Zheng Mechanism of the guanine nucleotide exchange reaction of Ras GTPase - evidence for a GTP/GDP displacement model Biochemistry 44 2005 2566 2576
18. E. Jacquet, S. Baouz, and A. Parmeggiani Characterization of mammalian CCDC25Mm exchange factor and kinetic properties of the exchange reaction intermediate p21.C-CDC25Mm Biochemistry 34 1995 12347 12354
19. J.L. Bos, J. de Rooij, and K.A. Reedquist Rap1 signalling: adhering to new models Nat. Rev. Mol. Cell. Biol. 2 2001 369 377
20. R.M. Wolthuis, and J.L. Bos Ras caught in another affair: the exchange factors for Ral Curr. Opin. Genet. Dev. 9 1999 112 117
21. E. Jacquet, M. Vanoni, C. Ferrari, L. Alberghina, E. Martegani, and A. Parmeggiani A mouse CDC25-like product enhances the formation of the active GTP complex of human ras p21 and Saccharomyces cerevisiae RAS2 proteins J. Biol. Chem. 267 1992 24181 24183
22. P. Bossu, M. Vanoni, V. Wanke, M.P. Cesaroni, F. Tropea, G. Melillo, C. Asti, S. Porzio, P. Ruggiero, V. Di Cioccio, G. Maurizi, A. Ciabini, and L. Alberghina A dominant negative RAS-specific guanine nucleotide exchange factor reverses neoplastic phenotype in K-ras transformed mouse fibroblasts Oncogene 19 2000 2147 2154
23. T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
24. R. Consonni, I. Arosio, T. Recca, R. Longhi, G. Colombo, and M. Vanoni Structure determination and dynamics of peptides overlapping the catalytic hairpin of the Ras-specific GEF Cdc25(Mm) Biochemistry 42 2003 12154 12162
25. L.A. Feig Ral-GTPases: approaching their 15 minutes of fame Trends Cell Biol. 13 2003 419 425
26. K. Burridge, and K. Wennerberg Rho and Rac take center stage Cell 116 2004 167 179
27. J.R. Sydor, M. Engelhard, A. Wittinghofer, R.S. Goody, and C. Herrmann Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex Biochemistry 37 1998 14292 14299
28. J. de Rooij, and J.L. Bos Minimal Ras-binding domain of Raf1 can be used as an activation-specific probe for Ras Oncogene 14 1997 623 625
29. J. Downward Targeting RAS signalling pathways in cancer therapy Nat. Rev. Cancer 3 2003 11 22
30. N. Guex, A. Diemand, and M.C. Peitsch Protein modelling for all Trends Biochem. Sci. 24 1999 364 367
31. J. Sambrook, E.F. Fritsch, and T. Maniatis Molecular Cloning: A Laboratory Manual 2nd edn. 1989 Cold Spring Harbor Laboratory Cold Spring Harbor, NY
32. B. Bauer, G. Mirey, I.R. Vetter, J.A. Garcia-Ranea, A. Valencia, A. Wittinghofer, J.H. Camonis, and R.H. Cool Effector recognition by the small GTP-binding proteins Ras and Ral J. Biol. Chem. 274 1999 17763 17770
33. R.H. Medema, R. Wubbolts, and J.L. Bos Two dominant inhibitory mutants of p21ras interfere with insulin-induced gene expression Mol. Cell. Biol. 11 1991 5963 5967
34. R. Zippel, C. De Maddalena, D. Porro, D. Modena, and M. Vanoni Int. J. Oncol. 4 1994 175 179
35. S.J. Taylor, and D. Shalloway Cell cycle-dependent activation of Ras Curr. Biol. 6 1996 1621 1627
36. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685