Relevance of the kinetic equilibrium of forces to the control of the cell cycle by Ras proteins

Biological Chemistry

Volumn 385, Issue 1, 2004, Pages 41-47

  Becker, Erwin W ^a  

^a KARLSRUHE INSTITUTE OF TECHNOLOGY   (Germany)

Author keywords

Cell transformation; Ras proteins; Signal transduction; Transfer of free energy

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; PHOSPHATE; PROTEIN KINASE; RAF PROTEIN; RAS PROTEIN; RHO FACTOR;

ALLOSTERISM; ARTICLE; CELL CYCLE; CELL DIVISION; CELL NUCLEUS; CONTROLLED STUDY; CYTOSKELETON; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME REGULATION; EXPERIMENTAL MODEL; HOMEOSTASIS; PHOSPHATE TRANSPORT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN HYDROLYSIS; PROTEIN MODIFICATION; SIGNAL TRANSDUCTION;

ANIMALS; CELL CYCLE; GUANOSINE DIPHOSPHATE; KINETICS; PROTO-ONCOGENE PROTEINS C-RAF; RAS GTPASE-ACTIVATING PROTEINS; RAS GUANINE NUCLEOTIDE EXCHANGE FACTORS; RAS PROTEINS; SIGNAL TRANSDUCTION;

EID: 1242343963     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.006     Document Type: Article

References (51)

1. Ahmadian, M.R., Hoffmann, U., Goody, R.S., and Wittinghofer, A. (1997). Individual rate constants for the interaction of Ras proteins with GTPase-activating proteins determined by fluorescence spectroscopy. Biochemistry 36, 4535-4541.
2. Allin, C., Ahmadian, M.R., Wittinghofer, A., and Gerwert, K. (2001). Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time. Proc. Natl. Acad. Sci. USA 98, 7754-7759.
3. Bagshaw, C.R., and Trentham, D.R. (1973). The reversibility of adenosine triphosphate cleavage by myosin. Biochem. J. 133, 323-328.
4. Bar-Sagi, D., and Hall, A. (2000). Ras and Rho GTPases: A family reunion. Cell 103, 227-238.
5. Becker, E.W. (2000). Kinetic equilibrium of forces and molecular events in muscle contraction. Proc. Natl. Acad. Sci. USA 97, 157-161.
6. Boguski, M.S., and McCormick, F. (1993). Proteins regulating Ras and its relatives. Nature 366, 643-654.
7. Boriack-Sjodin, P.A., Margarit, S.M., Bar-Sagi, D., and Kuriyan, J. (1998). The structural basis of the activation of Ras by Sos. Nature 394, 337-343.
8. Bourne, H.R., Sanders, D.A., and McCormick, F. (1990). The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132.
9. Bowtell, D., Fu, P., Simon, M., and Senior, P. (1992). Identification of murine homologues of the Drosophila Son of sevenless gene: potential activators of ras. Proc. Natl. Acad. Sci. USA 89, 6511-6515.
10. ras measured by a novel fluorescence anisotropy method. J. Biol. Chem. 268, 10914-10919,
11. Corbett, K.D., and Alber, T. (2001). The many faces of Ras: recognition of small GTP-binding proteins. Trends Biochem. Sci. 26, 710-716.
12. Fincham, V.J., Chudleigh, A., and Frame, M. C. (1999). Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 112, 947-956.
13. ras and in its complexes with the effector protein Raf-RBD and the GTPase activating protein GAP. Biochemistry 35, 10308-10320.
14. Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J.E., and Wittinghofer, A. (1992). Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12, 2050-2056.
15. Goody, R.S. (2003). The significance of the free energy of hydrolysis of GTP for signal-transducing and regulatory GTPases. Biophys. Chem. 100, 535-544.
16. Gorman, C., Skinner, R.H., Skelly, J.V., Neidle, S., and Lowe, P.N. (1996). Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf. J. Biol. Chem. 271, 6713-6719.
17. Helmreich, E.J.M. (2001). The Biochemistry of Cell Signalling (New York, USA: Oxford University Press).
18. ras and the Ras-binding domain of the human Raf-1 protein kinase. J. Biol. Chem. 270, 2901-2905.
19. John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., and Goody, R.S. (1990). Kinetics of interaction of nucleotides with nucleotide-free H-ras p 21. Biochemistry 29, 6058-6065.
20. Leevers, S.J., Paterson, H.F., and Marshall, C.J. (1994). Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369, 411-414.
21. Mm. Biochemistry 37, 7420-7430.
22. Maegley, K.A., Admiraal, S.J., and Herschlag, D. (1996). Ras-catalyzed hydrolysis of GTP: a new perspective from model studies. Proc. Natl. Acad. Sci. USA 93, 8160-8166.
23. Maehama, T., and Dixon, J.E. (1998). The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 13375-13378.
24. Marshall, C.J. (1996). Ras effectors. Curr. Op. Cell Biol. 8, 197-204.
25. McGlade, J., Brunkhorst, B., Anderson, D., Mbamalu, G., Settleman, J., Dedhar, S., Rozakis-Adcock, M., Chen, L. B., and Pawson, T. (1993). The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. EMBO J. 12, 3073-3081.
26. NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. Proc. Natl. Acad. Sci. USA 87, 3562-3565.
27. Nixon, A.E., Brune, M., Lowe, P.N., and Webb, M.R. (1995). Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin. Biochemistry 34, 15592-15598.
28. Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J., and Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
29. Pai, E.F., Krengel, U., Petsko, G.A., Goody, R.S., Kabsch, W., and Wittinghofer, A. (1990). Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359.
30. Rensland, H., John, J., Linke, R., Simon, I., Schlichting, I., Wittinghofer, A., and Goody, R.S. (1995). Substrate and product structural requirements for binding of nucleotides to H-ras p21: the mechanism of discrimination between guanosine and adenosine nucleotides. Biochemistry 34, 593-599.
31. Resat, H., Straatsma, T.P., Dixon, D.A., and Miller, J.H. (2001). The arginine finger of RasGAP helps GIn-61 align the nucleophilic water in GAP-stimulated hydrolysis of GTR Proc. Natl. Acad. Sci. USA 98, 6033-6038.
32. Rodriguez-Viciana, P., Warne, P.H., Khwaja, A., Marte, B.M., Pappin, D., Das, P., Waterfield, M.D., Ridley, A., and Downward, J. (1997). Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell 89, 457-467.
33. Rogge, R.D., Karlovich, C.A., and Banerjee, U. (1991). Genetic dissection of a neurodevelopmental pathway: son of sevenless functions downstream of the sevenless and EGF receptor tyrosine kinases. Cell 64, 39-48.
34. Scheffzek, K., Ahmadian, M.R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., and Wittinghofer A. (1997). The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338.
35. Schlessinger, J. (1993). How receptor tyrosine kinases activate Ras. TIBS 18, 273-275.
36. ras and other GTP-binding proteins. Nature Struct. Biol. 2, 36-44.
37. Settleman, J., Albright, C.F., Foster, L.C., and Weinberg, R.A. (1992). Association between GTPase activators for Rho and Ras families. Nature 359, 153-154.
38. ras-GTP: the catalytic conformation of the molecular switch II. Proteins 45, 297-312.
39. Spoerner, M., Herrmann, C., Vetter, I.R., Kalbitzer, H.R., and Wittinghofer, A. (2001). Dynamic properties of the Ras switch I region and its importance for binding to effectors. Proc. Natl. Acad. Sci. USA 98, 4944-4949.
40. Sprang, S.R. (1997). G Protein Mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678.
41. Stokoe, D., and McCormick, F. (1997). Activation of c-Raf-1 by Ras and Src through different mechanisms: activation in vivo and in vitro. EMBO J. 16, 2384-2396.
42. Stokoe, D., Macdonald, S.G., Cadwallader, K., Symons, M., and Hancock, J.F. (1994). Activation of Raf as a result of recruitment to the plasma membrane. Science 264, 1463-1467.
43. 31P solid state NMR spectroscopy. J. Mol. Biol. 323, 899-907.
44. Sydor, J.R., Engelhard, M., Wittinghofer, A., Goody, R.S., and Herrmann, C. (1998). 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, 14292-14299.
45. Tolkacheva, T., and Chan, A.M-L. (2000). Inhibition of H-Ras transformation by the PTEN/MMAC1/TEP1 tumor suppressor gene. Oncogene 19, 680-689.
46. Trahey, M., and McCormick, F. (1987). A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants. Science 238, 542-545.
47. Van Aelst, L., Barr, M., Marcus S., Polverino, A., and Wigler, M. (1993). Complex formation between RAS and RAF and other protein kinases. Proc. Natl. Acad. Sci. USA 90, 6213-6217.
48. Warne, P. H., Viciana, P.R., and Downward, J. (1993). Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 364, 352-355.
49. Wittinghofer, A., and Herrmann, C. (1995). Ras-effector interactions, the problem of specificity. FEBS Lett. 369, 52-56.
50. Wittinghofer, A., and Waldmann, H. (2000). Ras-a molecular switch involved in tumor formation. Angew. Chem. Int. Ed. in English 39, 4192-4214.
51. ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature 364, 308-313.