Identification of a novel mitogen-activated protein kinase kinase activation domain recognized by the inhibitor PD 184352

Molecular and Cellular Biology

Volumn 22, Issue 21, 2002, Pages 7593-7602

  Delaney, Amy M ^a   Printen, John A ^a   Chen, Huifen ^a   Fauman, Eric B ^a   Dudley, David T ^a  

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; CYCLIC AMP DEPENDENT PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; PHEROMONE; RAF PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; GENE OVEREXPRESSION; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BENZAMIDES; BLOTTING, WESTERN; CDC2 PROTEIN KINASE; CELL LINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; ENZYME INHIBITORS; GENE LIBRARY; HUMANS; INHIBITORY CONCENTRATION 50; MAP KINASE SIGNALING SYSTEM; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; MODELS, GENETIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

ANIMALIA; EUKARYOTA; MAMMALIA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0036837671     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.22.21.7593-7602.2002     Document Type: Article

References (33)

1. Alessi, D. R., A. Cuenda, P. Cohen, D. T. Dudley, and A. R. Saltiel. 1995. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:27489-27494.
2. raf-1. EMBO J. 13:1610-1619.
3. Bardwell, L., and J. Thorner. 1996. A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs. Trends Biochem. Sci. 21:373-374.
4. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12:849-859.
5. 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.
6. Catling, A. D., H. J. Schaeffer, C. W. Reuter, G. R. Reddy, and M. J. Weber. 1995. A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function. Mol. Cell. Biol. 15:5214-5225.
7. Cox, S., E. Radzio-Andzelm, and S. S. Taylor. 1994. Domain movements in protein kinases. Curr. Opin. Struct. Biol. 4:893-901.
8. Dang, A., J. A. Frost, and M. H. Cobb. 1998. The MEK1 proline-rich insert is required for efficient activation of the mitogen-activated protein kinases ERK1 and ERK2 in mammalian cells. J. Biol. Chem. 273:19909-19913.
9. Davies, S. P., H. Reddy, M. Caivano, and P. Cohen. 2000. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351:95-105.
10. Dhanasekaran, N., and E. Premkumar Reddy. 1998. Signaling by dual specificity kinases. Oncogene 17:1447-1455.
11. Dudley, D. T., L. Pang, S. J. Decker, A. J. Bridges, and A. R. Saltiel. 1995. A synthetic inhibitor of the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA 92:7686-7689.
12. Duesbery, N. S., C. P. Webb, S. H. Leppla, V. M. Gordon, K. R. Klimpel, T. D. Copeland, N. G. Ahn, M. K. Oskarsson, K. Fukasawa, K. D. Paull, and G. F. Vande Woude. 1998. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280:734-737.
13. Favata, M. F., K. Y. Horiuchi, E. J. Manos, A. J. Daulerio, D. A. Stradley, W. S. Feeser, D. E. Van-Dyk, W. J. Pitts, R. A. Earl, F. Hobbs, R. A. Copeland, R. L. Magolda, P. A. Scherle, and J. M. Trzaskos. 1999. Identification of a novel inhibitor of mitogen-activated protein kinase kinase. J. Biol. Chem. 273:18623-18632.
14. Frost, J. A., H. Steen, P. Shapiro, T. Lewis, N. Ahn, P. E. Shaw, and M. H. Cobb. 1997. Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. EMBO J. 16:6426-6438.
15. Fukuda, M., Y. Gotoh, and E. Nishida. 1997. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J. 16:1901-1908.
16. Hanks, S. K., and A. M. Quinn. 1991. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200:38-62.
17. Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
18. Kamakura, S., T. Moriguchi, and E. Nishida. 1999. Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus. J. Biol. Chem. 274:26563-26571.
19. Lorenz, M. C., R. S. Muir, E. Lim, J. McElver, S. C. Weber, and J. Heitman. 1995. Gene disruption with PCR products in Saccharomyces cerevisiae. Gene 158:113-117.
20. Mansour, S. J., J. M. Candia, J. E. Matsuura, M. C. Manning, and N. G. Ahn. 1996. Interdependent domains controlling the enzymatic activity of mitogen-activated protein kinase kinase 1. Biochemistry 35:15529-15536.
21. Mansour, S. J., W. T. Matten, A. S. Hermann, J. M. Candia, S. Rong, K. Fukasawa, G. F. Vande Woude, and N. G. Ahn. 1994. Transformation of mammalian cells by constitutively active MAP kinase kinase. Science 265:966-970.
22. Mody, N., J. Leitch, C. Armstrong, J. Dixon, and P. Cohen. 2001. Effects of MAP kinase cascade inhibitors on the MKK5/ERK5 pathway. FEBS Lett. 502:21-24.
23. Pearson, G., F. Robinson, T. Beers Gibson, B. Xu, M. Karandikar, K. Berman, and M. H. Cobb. 2001. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocrine Rev. 22:153-183.
24. Resing, K. A., and N. G. Ahn. 1998. Deuterium exchange mass spectrometry as a probe of protein kinase activation: analysis of wild-type and constitutively active mutants of MAP kinase kinase-1. Biochemistry 37:463-475.
25. Schaeffer, H. J., A. D. Catling, S. T. Eblen, L. S. Collier, A. Krauss, and M. J. Weber. 1998. MPI: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 281:1668-1671.
26. Sebolt-Leopold, J. S., D. T. Dudley, R. Herrera, K. Van Becelaere, A. Wiland, R. C. Gowan, H. Tecle, S. D. Barrett, A. Bridges, S. Przybranowski, W. R. Leopold, and A. R. Saltiel. 1999. Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo. Nat. Med. 5:810-816.
27. Shapiro, P. S., and N. G. Ahn. 1998. Feedback regulation of Raf-1 and mitogen-activated protein kinase (MAP) kinase kinases 1 and 2 by MAP kinase phosphatase-1 (MKP-1). J. Biol. Chem. 273:1788-1793.
28. Sherman, F., G. R. Fink, and J. B. Hicks. 1986. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
29. Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae, Genetics 122:19-27.
30. Stevenson, B. J., N. Rhodes, B. Errede, and G. F. Sprague, Jr. 1992. Constitutive mutants of the protein kinase STE11 activate the yeast pheromone response pathway in the absence of the G protein. Genes Dev. 6:1293-1304.
31. Tanoue, T., M. Adachi, T. Moriguchi, and E. Nishida. 2000. A conserved docking motif in MAP kinases common to substrates, activators and regulators. Nat. Cell. Biol. 2:110-116.
32. Taylor, S. S., and E. Radzio-Andzelm. 1994. Three protein kinase structures define a common motif. Structure 2:345-355.
33. Zheng, C. F., and K. L. Guan. 1993. Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases. J. Biol. Chem. 268:23933-23939.