Differential expression of MEK1 and MEK2 during mouse development

Cell Growth and Differentiation

Volumn 8, Issue 5, 1997, Pages 505-511

  Alessandrini, Alessandro ^b   Brott, Barbara K ^a,b   Erikson, Raymond L ^a  

^a HARVARD UNIVERSITY   (United States)

^b MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL EXPERIMENT; ARTICLE; CELL DIFFERENTIATION; CELL PROLIFERATION; EMBRYO DEVELOPMENT; GENE EXPRESSION REGULATION; GROWTH REGULATION; MITOGENICITY; MOUSE; NERVE CELL DIFFERENTIATION; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL;

ANIMALS; BLOTTING, NORTHERN; EMBRYONIC AND FETAL DEVELOPMENT; FEMALE; GENE EXPRESSION REGULATION, DEVELOPMENTAL; MAP KINASE KINASE 1; MAP KINASE KINASE 2; MICE; MITOGEN-ACTIVATED PROTEIN KINASE KINASES; PREGNANCY; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES;

ANIMALIA; MURINAE;

EID: 0030941898     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Blenis, J. Signal transduction via the MAP kinases: proceed at your own RSK. Proc. Natl. Acad. Sci. USA, 90: 5889-5892, 1993.
2. Seger, R., and Krebs, E. G. The MAPK signaling cascade. FASEB J., 9: 726-735, 1995.
3. Davis, R. J. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem., 268: 14553-14556, 1993.
4. Davis, R. J. MAPKs: new JNK expands the group. Trends Biochem. Sci., 19: 470-473, 1994.
5. Wu, J., Harrison, J. K., Dent, P., Lynch, K. R., Weber, M. J., and Sturgill, T. W. Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2. Mol. Cell. Biol., 13: 4539-4548, 1993.
6. Wu, J., Harrison, J. K., Vincent, L A., Haystead, C., Haystead, T. A. J., Michel, H., Hunt, D., Lynch, K. R., and Sturgill, T. W. Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase. Proc. Natl. Acad. Sci. USA, 90: 173-177, 1993.
7. Seger, R., Seger, D., Lozeman, F. J., Ahn, N. G., Graves, L. M., Campbell, J. S., Ericsson, L., Harrylock, M., Jensen, A. M., and Krebs, E. G. Human T-cell mitogen-activated protein kinase kinases are related to yeast signal transduction kinases. J. Biol. Chem., 267: 25628-25631, 1992.
8. Crews, C. M., Alessandrini, A. A., and Erikson, R. L. The primary structure of MEK, a protein kinase that phosphorylates the ERK gene product. Science (Washington DC), 258: 478-480, 1992.
9. Brott, B. K., Alessandrini, A., Largaespada, D. A., Copeland, N. G., Jenkins, N. A., Crews, C. M., and Erikson, R. L. MEK2 is a kinase related MEK1 and is differentially expressed in murine tissues. Cell Growth & Differ., 4: 921-929, 1993.
10. Zheng, C-F., and Guan, K-L. Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2. J. Biol. Chem., 268: 11435-11439, 1993.
11. Derijard, B., Raingeaud, J., Barret, T., Wu, I-H., Han, J., Ulevitch, R. J., and Davis, R. J. Independent human MAP kinase signal tansduction pathways defined by MEK and MKK isoforms. Science (Washington DC), 267: 682-685, 1995.
12. Sanchez, I., Hughes, R. T., Mayer, B. J., Yee, K., Woodgett, J. R., Avruch, J., Kyriakis, J. M., and Zon, L. I. Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun. Nature (Lond.), 372: 794-798, 1994.
13. Lin, A., Minden, A., Martinetto, H., Claret, F-X., Lange-Carter, C., Mercurio, F., Johnson, G. H., and Karin, M. Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2. Science (Washington DC), 268: 286-290, 1995.
14. Zhou, G., Boa, Z. B., and Dixon, J. E. Components of a new human protein kinase signal transduction pathway. J. Biol. Chem., 270: 12665-12669, 1995.
15. English, J. M., Vanderbilt, C. A., S., X., Marcus, S., and Cobb, M. H. Isolation of MEK5 and differential expression of alternatively spliced forms. J. Biol. Chem. 270: 28897-28902, 1995.
16. Han, J., Lee, J-D., Jiang, Y., Li, Z., Feng, L., and Ulevitch, R. J. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J. Biol. Chem., 271: 2886-2891, 1996.
17. Zheng, C-F., and Guan, K-L. Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases. J. Biol. Chem., 268: 23933-23939, 1993.
18. Wu, X., Noh, S. J., Zhou, G., Dixon, J. E., and Guan, K-L. Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells. J. Biol. Chem., 271: 3265-3271, 1996.
19. Jelenik, T., Catling, A. D., Reuter, C. W. M., Moodie, S. A., Wolfman, A., and Weber, M. J. RAS and RAF-1 form a signalling complex with MEK-1 but not MEK-2. Mol. Cell. Biol., 14: 8212-8218, 1994.
20. Catling, A. D., Schaeffer, H-J., Reuter, C. W. M., Reddy, G. R., and Weber, M. J. A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function. Mol. Cell. Biol., 15: 5214-5225, 1995.
21. Downey, G. P., Butler, J. R., Brumell, J., Borregaard, N., Kjeldsen, L., Sue-A-Quan, A., and Grinstein, S. Chemotactic peptide-induced activation of MEK-2, the predominant isoform in human neutrophils. J. Biol. Chem., 271: 21005-21011, 1996.
22. Cowley, S., Paterson, H., Kemp, P., and Marshall, C. J. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH3T3 cells. Cell, 77: 841-852, 1994.
23. Wilkinson, D. G., Bailes, J. A., Champion, J. E., and McMahon, A. P. A molecular analysis of mouse development from 8 to 10 days post coitum detects changes only in embryonic globin expression. Development (Camb.), 99: 493-500, 1987.
24. Echelard, Y., Epstein, D. J., St.-Jacques, B., Shen, L., Mohler, J., McMahon, J. A., and McMahon, A. P. Sonic hedgehog, a member of a family of putative signaling molecules, is implicated in the regulation of CNS and limb polarity. Cell, 75: 1417-1430, 1993.
25. Alessandrini, A., Crews, C. M., and Erikson, R. L. Phorbol ester stimulates a protein tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product. Proc. Natl. Acad. Sci. USA, 89: 8200-8204, 1992.