Phosphorylation of αB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation

Journal of Biological Chemistry

Volumn 273, Issue 43, 1998, Pages 28346-28354

  Kato, Kanefusa ^a   Ito, Hidenori ^a   Kamei, Keiko ^a   Inaguma, Yutaka ^a   Iwamototo, Ikuko ^a   Sagal, Shinsuke ^b  

^a INSTITUTE FOR DEVELOPMENTAL RESEARCH   (Japan)

^b AICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BETA CRYSTALLIN; CALYCULIN A; HEAT SHOCK PROTEIN 27; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; MYELIN BASIC PROTEIN; PROTEIN KINASE; SERINE; CRYSTALLIN; MAP KINASE ACTIVATED KINASE 2; MAP-KINASE-ACTIVATED KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE 1; PEPTIDE FRAGMENT; PHOSPHOPROTEIN; PROTEIN SERINE THREONINE KINASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GLIOMA CELL; HUMAN; HUMAN CELL; IMMUNOBLOTTING; ISOELECTRIC FOCUSING; MITOSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; ANIMAL; CELL COMPARTMENTALIZATION; CELL CULTURE; ENZYME SPECIFICITY; ISOLATION AND PURIFICATION; METABOLISM; MOUSE; PHOSPHORYLATION; RABBIT;

ANIMALS; CELL COMPARTMENTATION; CRYSTALLINS; HUMANS; MICE; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOSIS; PEPTIDE FRAGMENTS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; RABBITS; SERINE; SUBSTRATE SPECIFICITY; TUMOR CELLS, CULTURED;

EID: 0032561079     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.43.28346     Document Type: Article

References (35)

1. Wistow, G. J., and Piatigorsky, J. (1988) Annu. Rev. Biochem. 57, 479-504
2. Voorter, C. E., Mulders, J. W., Bloemendal, H., and de Jong, W. W. (1986) Eur. J. Biochem. 160, 203-210
3. Chiesa, R., Gawinowicz-Kolks, M. A., and Spector, A. (1987) J. Biol. Chem. 262, 1438-1441
4. Van Der Ouderaa, F. J., de Jong, W. W., Hilderink, A., and Bloemendal, H. (1974) Eur. J. Biochem. 49, 157-168
5. de Jong, W. W., Leunissen, J. A., and Voorter, C. E. (1993) Mol. Biol. Evol. 10, 103-126
6. Kato, K., Goto, S., Inaguma, Y., Hasegawa, K., Morishita, R., and Asano, T. (1994) J. Biol. Chem. 269, 15302-15309
7. Caspers, G.-J., Leunissen, J. A. M., and de Jong, W. W. (1995) J. Mol. Evol. 40, 238-248
8. Ehrnsperger, M., Gaestel, M., and Buchner, J. (1997) in Molecular Chaperones in the Life Cycle of Proteins (Fink, A. L., and Goto, Y., eds) pp. 533-575, Marcel Dekker, Inc., New York
9. Kato, K., Shinohara, H., Goto, S., Inaguma, Y., Morishita, R., and Asano, T. (1992) J. Biol. Chem. 267, 7718-7725
10. Kato, K., Shinohara, H., Kurobe, N., Goto, S., Inaguma, Y., and Ohshima, K. (1991) Biochim. Biophys. Acta 1080, 173-180
11. Kato, K., Shinohara, H., Kurobe, N., Inaguma, Y., Shimizu, K., and Ohshima, K. (1991) Biochim. Biophys. Acta 1074, 201-208
12. Klemenz, R., Fröhli, E., Steiger, R. H., Schäfer, R., and Aoyama, A. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 3652-3656
13. Inaguma, Y., Shinohara, H., Goto, S., and Kato, K. (1991) Biochem. Biophys. Res. Commun. 182, 844-850
14. Arrigo, A.-P., and Welch, W. J. (1987) J. Biol. Chem. 262, 15359-15369
15. Landry, J., Chretien, P., Laszlo, A., and Lambert, H. (1991) J. Cell. Physiol. 147, 93-101
16. Landry, J., Lambert, H., Zhou, M., Lavoie, J. N., Hickey, E., Weber, L. A., and Anderson, C. W. (1992) J. Biol. Chem. 267, 794-803
17. Beall, A. C., Kato, K., Goldenring, J. R., Rasmussen, H., and Brophy, C. M. (1997) J. Biol. Chem. 272, 11283-11287
18. Chiesa, R., Gawinowicz-Kolks, M. A., Kleiman, N. J., and Spector, A. (1987) Biochem. Biaphys. Res. Commun. 144, 1340-1347
19. Chiesa, R., Gawinowicz-Kolks, M. A., Kleiman, N. J., and Spector, A. (1988) Exp. Eye Res. 46, 199-208
20. Smith, J. B., Sun, Y., Smith, D. L., and Green, B. (1992) Protein. Sci. 1, 601-608
21. Spector, A., Chiesa, R., Sredy, J., and Garner, W. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 4712-4716
22. Kantorow, M., and Piatigorsky, J. (1994) Proc. Natl. Acad. Sci. U. S.A. 91, 3112-3116
23. Kantorow, M., Horwitz, J., van Boekel, M. A. M., de Jong, W. W., and Piatigorsky, J. (1995) J. Biol. Chem. 270, 17215-17220
24. Ito, H., Okamoto, K., Hakayama, H., Isobe, T., and Kato, K. (1997) J. Biol. Chem. 272, 29934-29941
25. Kimura, G., and Itagaki, A. (1975) Proc. Natl. Acad. Sci. U. S. A. 72, 673-677
26. Zieve, G. W., Turnbull, D., Mullins, J. M., and Mcintosh, R. (1980) Exp. Cell Res. 126, 397-405
27. Kato, K., Ito, H., Inaguma, Y., Okamoto, K., and Saga, S. (1996) J. Biol. Chem. 271, 26989-26994
28. Kozaki, K., Miyaishi, O., Koiwai, O., Yasui, Y., Kashiwai, A., Nishikawa, Y. Shimizu, S., and Saga, S. (1998) J. Biol. Chem. 273, 15125-15130
29. Laemmli, U. K. (1970) Nature 227, 680-685
30. Schägger, H., and von Jagow, G. (1987) Anal. Biochem. 166, 368-379
31. O'Farrell, P. H. (1975) J. Biol. Chem. 250, 4007-4021
32. Yoshitake, S., Yamada, Y., Ishikawa, E., and Masseyeff, R. (1979) Eur. J. Biochem. 101, 395-399
33. Bloemendal, H., and Groenewoud, G. (1981) Anal. Biochem. 117, 327-329
34. Dudley, D. T., Pang, L., Decker, S. J., Bridges, A. J., and Saltiel, A. R. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 7686-7689
35. Lee, J. C., Laydon, J. T., McDonnell, P. C., Gallagher, T. P., Kumar, S., Green, D., McNulty, D., Blumenthal, M. J., Heys, J. R., Landvatter, W., Strickler, J. E., McLaughlin, M. M., Siemens, I. R., Fisher, S. M., Livi, G. P., White, J. R., Adams, J. L., and Young, P. R. (1994) Nature 372, 739-746