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Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase
Open accessAbstract
A growth factor-stimulated (MAP2-related) protein kinase, ERT, that phosphorylates the epidermal growth factor receptor at Thr669 has been purified from KB human tumor cells by Northwood and co-workers (Northwood, I. C., Gonzalez, F. A., Wartmann, M., Raden, D. L., and Davis, R. J. (1991) J. Biol. Chem. 266, 15266-15276). The ERT protein kinase has a restricted substrate specificity, and the structural determinants employed for substrate recognition by this enzyme have not been defined. As an approach toward understanding the specificity of substrate phosphorylation, we have used an in vitro assay to identify additional substrates for the ERT protein kinase. In this report we describe two novel substrates: (a) the human c-myc protein at Ser62 and (b) the rat c-jun protein at Ser246. Alignment of the primary sequences surrounding the phosphorylation sites located within the epidermal growth factor receptor (Thr669), Myc (Ser62), and Jun (Ser246) demonstrated a marked similarity. The observed consensus sequence was Pro-Leu-Ser/Thr-Pro. We propose that this sequence forms part of a substrate structure that is recognized by the ERT protein kinase.
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Cited by
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Self-citationHibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Bowman, T., Garcia, R., Turkson, J., & Jove, R. (2000) · Oncogene · doi:10.1038/sj.onc.1203527 · Cited by 1,743
Kallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2996 · Cited by 642
Self-citationKeshet, Y., & Seger, R. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-795-2_1 · Cited by 642
Caldenhoven, E., van Dijk, T. B., Solari, R., Armstrong, J., Raaijmakers, J. A. M., Lammers, J.-W. J., Koenderman, L., & de Groot, R. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13221 · Cited by 373
Yang, B.-S., Hauser, C. A., Henkel, G., Colman, M. S., Beveren, C. V., Stacey, K. J., Hume, D. A., Maki, R. A., & Ostrowski, M. C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.538 · Cited by 333
The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution
Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275
Minden, A., Lin, A., Smeal, T., Dérijard, B., Cobb, M., Davis, R., & Karin, M. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6683 · Cited by 195
Self-citationBüscher, D., Hipskind, R. A., Krautwald, S., Reimann, T., & Baccarini, M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.1.466 · Cited by 176
A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells*
Stuart, S. A., Houel, S., Lee, T., Wang, N., Old, W. M., & Ahn, N. G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047233 · Cited by 116
Metadata
- Authors
- Alvarez, E., Northwood, I. C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., & Davis, R. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-08
- Volume
- 266
- Issue
- 23
- Pages
- 15277-15285
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1504158642
- Cited by
- 472
- References
- 0
- FWCI
- 23.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
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