Negative regulation of Raf-1 by phosphorylation of serine 621

Molecular and Cellular Biology

Volumn 16, Issue 10, 1996, Pages 5409-5418

  Mischak, Harald ^a   Seitz, Thomas ^a   Janosch, Petra ^a   Eulitz, Manfred ^a   Steen, Helge ^b   Schellerer, Miriam ^a   Philipp, Alex ^a   Kolch, Walter ^a  

^a INSTITUTE OF EPIDEMIOLOGY   (Germany)

^b MAX PLANCK INSTITUTE OF IMMUNOBIOLOGY AND EPIGENETICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYSTEINE; GUANOSINE TRIPHOSPHATE; RAF PROTEIN; RAS PROTEIN; SERINE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CATALYSIS; CELL STRAIN COS1; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION;

ANIMALIA; INSECTA;

EID: 0029810302     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.10.5409     Document Type: Article

References (52)

1. Bruder, J. T., G. Heidecker, and U. R. Rapp. 1992. Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase. Genes Dev. 6:545-556.
2. Burgering, B. M., G. J. Pronk, P. C. van Weeren, P. Chardin, and J. L. Bos. 1993. cAMP antagonizes p21ras-directed activation of extracellular signal-regulated kinase 2 and phosphorylation of mSos nucleotide exchange factor. EMBO J. 12:4211-4220.
3. Carroll, M. P., and W. S. May. 1994. Protein kinase C-mediated serine phosphorylation directly activates Raf-1 in murine hematopoietic cells. J. Biol. Chem. 269:1249-1256.
4. Chow, Y.-H., K. Pumiglia, T. H. Jun, P. Dent, T. W. Sturgill, and R. Jove. 1995. Functional mapping of the N-terminal regulatory domain in the human Raf-1 protein kinase. J. Biol. Chem. 270:14100-14106.
5. Chuang, E., D. Barnard, L. Hettich, X. F. Zhang, J. Avruch, and M. S. Marshall. 1994. Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues. Mol. Cell. Biol. 14:5318-5325.
6. Clanton, D. J., Y. Y. Lu, D. G. Blair, and T. Y. Shin. 1987. Structural significance of the GTP-binding domain of ras p21 studied by site-directed mutagenesis. Mol. Cell. Biol. 7:3092-3097.
7. Cook, S. J., and F. McCormick. 1993. Inhibition by cAMP of Ras-dependent activation of Raf. Science 262:1069-1072.
8. Cowley, S., H. Paterson, P. Kemp, and C. J. Marshall. 1994. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell 77:841-852.
9. Daum, G., I. Eisenmann-Tappe, H.-W. Fries, J. Troppmair, and U. R. Rapp. 1994. The ins and outs of Raf kinases. Trends Biochem. Sci. 19:474-480.
10. Davis, R. 1994. MAPKs: new JNK expands the group. Trends Biochem. Sci. 19:470-473.
11. Dent, P., T. Jelinek, D. K. Morrison, Vl. J. Weber, and T. W. Sturgill. 1995. Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science 268:1902-1906.
12. Dent, P., D. B. Reardon, D. K. Morrison, and T. W. Sturgill. 1995. Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro. Mol. Cell. Biol. 15:4125-4135.
13. ai/o subunits. J. Biol. Chem. 271:3119-3123.
14. Dent, P., and T. W. Sturgill. 1994. Activation of (His)6-Raf-1 in vitro by partially purified plasma membranes from v-Ras transformed and scrumstimulated fibroblasts. Proc. Natl. Acad. Sci. USA 91:9544-9548.
15. Fabian, J. R., I. O. Daar, and D. K. Morrison. 1993. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell. Biol. 13:7170-7179.
16. Fabian, J. R., A. B. Vojtek, J. A. Cooper, and D. K. Morrison. 1994. A single amino acid change in Raf-1 inhibits Ras binding and alters Raf-1 function. Proc. Natl. Acad. Sci. USA 91:5982-5986.
17. Graves, L. M., K. E. Bornfeldt, E. W. Raines, B. C. Potts, S. G. Macdonald, R. Ross, and E. G. Krebs. 1993. Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells. Proc. Natl. Acad. Sci. USA 90:10300-10304.
18. Guan, K. L., and J. E. Dixon. 1991. Eucaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione.S-transferase. Anal. Biochem. 192:262-267.
19. Häfner, S., H. S. Adler, H. Mischak, P. Janosch, G. Heidecker, A. Wolfman, S. Pippig, M. Lohse, M. Ueffing, and W. Kolch. 1994. Mechanism of inhibition of Raf-1 by protein kinase A. Mol. Cell. Biol. 14:6696-6703.
20. Heidecker, G., W. Kolch, D. K. Morrison, and U. R. Rapp. 1992. The role of Raf-1 phosphorylation in signal transduction. Adv. Cancer Res. 58:53-73.
21. ras-mitogen-activated protein kinase pathway in fibroblasts. J. Biol. Chem. 269:3534-3538.
22. Hou, X. S., T. B. Chou, M. B. Melnick, and N. Perrinton. 1995. The torso receptor tyrosine kinase can activate Raf in a Ras-independent pathway. Cell 81:63-71.
23. Jelinek, T., P. Dent, T. W. Sturgill, and M. J. Weber. 1995. Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol. Cell. Biol. 16:1027-1034.
24. Kolch, W., G. Heidecker, G. Kochs, R. Hummel, H. Vahidi, H. Mischak, G. Finkenzeller, D. Marine, and U. R. Rapp. 1993a. PKCa activates Raf-1 by direct phosphorylation. Nature (London) 364:249-251.
25. Kolch, W., G. Heidecker, P. Lloyd, and U. R. Rapp. 1991. Raf-1 protein kinase is required for growth of induced NIH/3T3 cells. Nature (London) 349:426-428.
26. Kolch, W., G. Heidecker, J. Troppmair, K. Yanagihara, R. H. Bassin, and U. R. Rapp. 1993b. Raf revertant cells resist transformation by non-nuclear oncogenes and are deficient in the induction of early response genes by TPA and serum. Oncogene 8:361-370.
27. Leevers, S. J., H. F. Paterson, and C. J. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature (London) 369:411-414.
28. Li, S., P. Janosch, M. Tanji, G. C. Rosenfeld, J. C. Waymire, H. Mischak, W. Kolch, and J. M. Sedivy. 1995. Regulation of Raf-1 kinase activity by the 14-3-3 family of proteins. EMBO J. 14:685-696.
29. Marais, R., Y. Light, H. F. Paterson, and C. J. Marshall. 1995. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14:3136-3145.
30. Marshall, C. J. 1994. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev. 4:82-89.
31. Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
32. McKnight, G. S. 1991. Cyclic AMP second messenger systems. Curr. Opin. Cell Biol. 3:213-217.
33. Menini, A. 1995. Cyclic nucleotide-gated channels in visual and olfactory transduction. Biophys. Chem. 55:185-196.
34. Michaud, N. R., J. R. Fabian, K. D. Mathes, and D. K. Morrison. 1995. 14-3-3 is not essential for Raf-1 function: identification of Raf-1 proteins that are biologically activated in a 14-3-3- and Ras-independent manner. Mol. Cell. Biol. 15:3390-3397.
35. Moodie, S. A., and A. Wolfman. 1994. The 3Rs of life: Ras, Raf and growth regulation. Trends Genet. 10:44-48.
36. Morrison, D. K. 1994. 14-3-3: modulators of signaling proteins? Science 266:56-57.
37. Morrison, D. K., G. Heidecker, U. R. Rapp, and T. D. Copeland. 1993. Identitication of the major phosphorylation sites of the Raf-1 kinase. J. Biol. Chem. 268:17309-17316.
38. Muslin, A. J., J. W. Tanner, P. M. Allen, and A. S. Shaw. 1996. Interaction of 14-3-3 with signalling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897.
39. Philipp, A., H. Mischak, and W. Kolch. 1995. Unpublished data.
40. Piper, R. C., D. E. James, J. W. Slot, C. Puri, and J. C. Lawrence. 1993. GLUT4 phosphorylation and inhibition of glucose transport by dibutyryl cAMP. J. Biol. Chem. 268:16557-16563.
41. Rommel, C., G. Radziwill, J. Lovric, J. Noeldeke, T. Heinicke, D. Jones, A. Aitken, and K. Moelling. 1996. Activated Ras displaces 14-3-3 protein from the amino terminus of c-Raf-1. Oncogene 12:609-619.
42. Russell, M., S. Winitz, and G. L. Johnson. 1994. Acetylcholine muscarinic ml receptor regulation of cyclic AMP synthesis controls growth factor stimulation of Raf activity. Mol. Cell. Biol. 14:2343-2351.
43. Sozeri, O., K. Vollmer, M. Liyanage, D. Frith, G. Kour, G. E. Mark, and S. Stabel. 1992. Activation of the c-Raf protein kinase by protein kinase C phosphorylation. Oncogene 7:2259-2262.
44. Stokoe, D., S. G. Macdonald, K. Cadwallader, M. Symons, and J. F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467.
45. Svetson, B. R., X. Kong, and J. C. Lawrence, Jr. 1993. Increasing cAMP attenuates activation of mitogen-activated protein kinase. Proc. Natl. Acad. Sci. USA 990:1030.5-10309.
46. Traverse, S., P. Cohen, H. Paterson, C. Marshall, U. R. Rapp, and R. J. A. Grand. 1993. Specific association of activated MAP kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells. Oncogene 8:3175-3181.
47. Uhler, M. D., and G. S. McKnight. 1987. Expression of cDNAs for two isoforms of the catalytic subunit of cAMP-dependent protein kinase. J. Biol. Chem. 262:15202-15207.
48. Varnum, M. D., K. D. Black, and W. N. Zagotta. 1995. Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels. Neuron 15: 619-625.
49. Whiteburst, C. E., H. Owaki, J. T. Bruder, U. R. Rapp, and T. D. Geppert. 1995. The MEK kinase activity of the catalytic domain of RAF-1 is regulated independently of Ras binding in T cells. J. Biol. Chem. 270:5594-5599.
50. Williams, N. G., and T. M. Roberts. 1994. Signal transduction pathways involving the Raf proto-oncogene. Cancer Metastasis Rev. 13:105-116.
51. Williams, N. G., T. M. Roberts, and P. Li. 1992. Both p21ras and pp60v-src are required, but neither alone is sufficient, to activate the Raf-1 kinase. Proc. Natl. Acad. Sci. USA 89:2922-2926.
52. Wu, J., P. Dent, T. Jelinek, A. Wolfman, M. J. Weber, and T. W. Sturgill. 1993. Inhibition of the EGF-activated MAP kinase signaling pathway by adenosine 3′,5′-monophosphate. Science 262:1065-1069.