Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer

Journal of Biological Chemistry

Volumn 277, Issue 39, 2002, Pages 36465-36470

  Kim, Soyoun ^a,b   Zagozdzon, Radoslaw ^a,b   Meisler, Alan ^a,b   Baleja, James D ^a,b   Fu, Yigong ^a,b   Avraham, Shalom ^a,b   Avraham, Hava ^a,b,c  

^a HARVARD MEDICAL SCHOOL   (United States)

^b TUFTS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c HARVARD INSTITUTES OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITION; NUCLEAR MAGNETIC RESONANCE; PROTEINS; TUMORS;

GROWTH REGULATORS;

BIOCHEMISTRY;

CSK HOMOLOGOUS KINASE; NEU DIFFERENTIATION FACTOR; PROTEIN KINASE; PROTEIN TYROSINE KINASE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BREAST CANCER; CANCER INHIBITION; ENZYME ACTIVITY; ENZYME INHIBITION; GENE THERAPY; GROWTH REGULATION; HUMAN; HUMAN CELL; ONCOGENE NEU; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; BREAST NEOPLASMS; CELL DIVISION; GENETIC VECTORS; GLUTATHIONE TRANSFERASE; HUMANS; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE BIOSYNTHESIS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS PP60(C-SRC); RECEPTOR, ERBB-2; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; TUMOR CELLS, CULTURED;

EID: 0037184030     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206018200     Document Type: Article

References (34)

1. Borg, A., Sigurdsson, H., Clark, G. M., Ferno, M., Fuqua, S. A., Olsson, H., Killander, D., and McGurie, W. L. (1991) Br. J. Cancer 63, 136-142
2. Newman, B., Austin, M. A., Lee, M., and King, M. C. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 3044-3048
3. Bishop, J. M. (1995) Genes Dev. 9, 1309-1315
4. Yamamoto, T., Ikawa, S., Akiyama, T., Semba, K., Nomura, N., Miyajima, N., Saito, T., and Toyoshima, K. (1986) Nature 319, 230-234
5. Menard, S., Tagliabue, E., Campiglio, M., and Pupa, S. M. (2000) J. Cell. Physiol. 182, 150-162
6. Muthuswamy, S. K., and Muller, W. J. (1995) Oncogene 11, 1801-1810
7. Muthuswamy, S. K., and Muller, W. J. (1995) Oncogene 11, 271-279
8. Di Fiore, P. P., Pierce, J. H., Kraus, M. H., Segatto, O., King, C. R., and Aaronson, S. A. (1987) Science 237, 178-182
9. Ben-Levy, R., Peles, E., Goldman-Michael, R., and Yarden, Y. (1992) J. Biol. Chem. 267, 17304-17313
10. Ben-Levy, R., Paterson, H. F., Marshall, C. J., and Yarden, Y. (1994) EMBO J. 13, 3302-3311
11. Dankort, D. L., Wang, Z., Blackmore, V., Moran, M. F., and Muller, W. J. (1997) Mol. Cell. Biol. 17, 5410-5425
12. Akiyama, T., Matsuda, S., Namba, Y., Saito, T., Toyoshima, K., and Yamamoto, T. (1991) Mol. Cell. Biol. 11, 833-842
13. Zrihan-Licht, S., Lim, J., Keydar, I., Sliwkowski, M. X., Groopman, J. E., and Avraham, H. (1997) J. Biol. Chem. 272, 1856-1863
14. Zrihan-Licht, S., Deng, B., Yarden, Y., McShan, G., Keydar, I., and Avraham, H. (1998) J. Biol. Chem. 273, 4065-4072
15. Bougeret, C., Jiang, S., Keydar, I., and Avraham, H. (2001) J. Biol. Chem. 276, 33711-33720
16. Klages, S., Adam, D., Class, K., Fargnoli, J., Bolen, J. B., and Penhallow, R. C. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 2597-2601
17. Chow, L. M., Jarvis, C., Hu, Q., Nye, S. H., Gervais, F. G., Veillette, A., and Matis, L. A. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 4975-4979
18. Davidson, D., Chow, L. M., and Veillette, A. (1997) J. Biol. Chem. 272, 1355-1362
19. Gibbs, J. B. (2000) Science 287, 1969-1973
20. Waksman, G., Kominos, D., Robertson, S. C., Pant, N., Baltimore, D., Birge, R. B., Cowburn, D., Hanafusa, H., Mayer, B. J., and Overduin, M. (1992) Nature 358, 646-653
21. Waksman, G., Shoelson, S. E., Pant, N., Cowburn, D., and Kuriyan, J. (1993) Cell 72, 779-790
22. Xu, W., Harrison, S. C., and Eck, M. J. (1997) Nature 385, 595-602
23. Kay, L. E., Muhandiram, D. R., Wolf, G., Shoelson, S. E., and Forman-Kay, J. D. (1998) Nat. Struct. Biol. 5, 156-163
24. Kim, S., Cullis, D. N., Feig, L. A., and Baleja, J. D. (2001) Biochemistry 40, 6776-6785
25. Rajagopal, P., Waygood, E. B., Reizer, J., Saier, M. H., Jr., and Klevit, R. E. (1997) Protein Sci. 6, 2624-2627
26. Matsuo, H., Kupce, E., Li, H., and Wagner, G. (1996) J. Magn. Reson. 113, 190-194
27. Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., and Sykes, B. D. (1995) J. Biomol. NMR 5, 67-81
28. Thomas, S. M., and Brugge, J. S. (1997) Annu. Rev. Cell Dev. Biol. 13, 513-609
29. Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G., Pawson, T., Haser, W. G., King, F., Roberts, T., Ratnofsky, S., and Lechleider, R. J. (1993) Cell 72, 767-778
30. Hoedemaeker, F. J., Siegal, G., Roe, S. M., Driscoll, P. C., and Abrahams, J. P. (1999) J. Mol. Biol. 292, 763-770
31. Bradshaw, J. M., Mitaxov, V., and Waksman, G. (1999) J. Mol. Biol. 293, 971-985
32. Mainville, C., A., Parmar, K., Unnikrishnan, I., Gong, L., Raffel, G. D., and Rosenberg, N. (2001) J. Virol. 75, 1816-1823
33. Mattson, P. T., Lappalainen, I., Backesjo, C. M., Brockman, E., Lauren, S., Vihinen, M., and Smith, C. I. (2000) J. Immunol. 164, 4170-4177
34. Murthy, T. V. S., and Webster, G. D. (2001) Protein Data Bank (www.rcsb.org/pdb