Thr94 in Bovine Myelin Basic Protein Is a Second Phosphorylation Site for 42-kDa Mitogen-Activated Protein Kinase (ERK2)

Journal of Protein Chemistry

Volumn 22, Issue 2, 2003, Pages 177-181

  Hirschberg, Daniel ^a   Rådmark, Olof ^a   Jörnvall, Hans ^a   Bergman, Tomas ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Electrospray ionization electrospray ionization mass spectrometry; Extracellular signal regulated kinase 2; Matrix assisted laser desorption ionization mass spectrometry; Mitogen activated protein kinase; Myelin basic protein; Phosphorylation

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARAGINYLISOLEUCYLVALYLTHREONYLPROLYLARGINYLTHREONYLPROLYLPROLYLPROLYLSER INE; FUNCTIONAL GROUP; MAGNESIUM ION; MITOGEN ACTIVATED PROTEIN KINASE 1; MYELIN BASIC PROTEIN; PEPTIDE FRAGMENT; PHOSPHATE; PROLINE DIRECTED PROTEIN KINASE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; CATTLE; ENZYME PHOSPHORYLATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; TANDEM MASS SPECTROMETRY;

ANIMALS; BINDING SITES; BRAIN CHEMISTRY; CATTLE; MITOGEN-ACTIVATED PROTEIN KINASE 1; MYELIN BASIC PROTEINS; PEPTIDE FRAGMENTS; PHOSPHORYLATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THREONINE; TRYPSIN;

BOS TAURUS; BOVINAE;

EID: 0346079910     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023479131488     Document Type: Article

References (18)

1. Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radziejewska, E., Morgenbesser, S. D., et al. (1991). Cell 65: 663-675.
2. Chou, F. C.-H., Chou, C.-H. J., Shapira, R., and Kibler, R. F. (1976). J. Biol. Chem. 251: 2671-2679.
3. Cohen, P. (2002). Nat. Rev. Drug Discov. 1: 309-315.
4. Erickson, A. K., Payne, D. M., Martino, P. A., Rossomando, A. J., Shabanowitz, J., Weber, M. J., et al. (1990). J. Biol Chem. 265: 19728-19735.
5. Eylar, E. H., Brostoff, S. W., Hashim, G., Caccam, J., and Burnett, P. (1971). J. Biol. Chem. 246: 5770-5784.
6. Gonzalez, F. A., Raden, D. L., and Davis, R. J. (1991). J. Biol. Chem. 266: 22159-22163.
7. Johnson, E. M., Maeno, H., and Greengard, P. (1971). J. Biol. Chem. 246: 7731-7739.
8. Payne, D. M., Rossomando, A. J., Martino, P., Erickson, A. K., Her, J. H., Shabanowitz, J., et al. (1991). EMBO J. 10: 885-892.
9. Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, A. R., and Anderton, B. H. (2000). J. Neurochem. 74: 1587-1595.
10. Rossomando, A. J., Payne, D. M., Weber, M. J., and Sturgill, T. W. (1989). Proc. Natl. Acad. Sci. USA 86: 6940-6943.
11. Rossomando, A. J., Sanghera, J. S., Marsden, L. A., Weber, M. J., Pelech, S. L., and Sturgill, T. W. (1991). J. Biol. Chem. 266: 20270-20275.
12. Sanghera, J. S., Aebersold, R., Morrison, H. D., Bures, E. J., and Pelech, S. L. (1990). FEBS Lett. 273: 223-226.
13. Shoji, S., Ohnishi, J., Funakoshi, T., Fukunaga, K., Miyamoto, E., Ueki, H., et al. (1987). J. Biochem. 102: 1113-1120.
14. Smith, R. (1980). Biochemistry 19: 1826-1831.
15. Ulmer, J. B. (1988). Prog. Neurobiol. 31: 241-259.
16. Weiwad, M., Küllertz, G., Schutkowski, M., and Fischer, G. (2000). FEBS Lett. 478: 39-42.
17. Yu, J.-S., and Yang, S.-D. (1994). J. Neurochem. 62: 1596-1603.
18. Zand, R., Li, M. X., Jin, X., and Lubman, D. (1998). Biochemistry 37: 2441-2449.