Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1α

Cancer Research

Volumn 62, Issue 22, 2002, Pages 6357-6361

  Liu, Ying ^a   Virshup, David M ^a   White, Raymond L ^a   Hsu, Lih Ching ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BRCA1 PROTEIN; GLUTATHIONE TRANSFERASE; PHOSPHOPROTEIN PHOSPHATASE 2A;

ANIMAL CELL; ARTICLE; CELL CYCLE G1 PHASE; CHROMOSOME SEGREGATION; DNA DAMAGE; DNA REPAIR; DNA STRAND BREAKAGE; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE; GAMMA IRRADIATION; GENE MUTATION; NONHUMAN; OVARY CANCER; PRIORITY JOURNAL; TUMOR SUPPRESSOR GENE;

ANIMALS; BRCA1 PROTEIN; CATALYSIS; COS CELLS; GLUTATHIONE TRANSFERASE; HUMANS; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT PROTEINS;

EID: 0037112506     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (26)

1. Welcsh, P. L., and King, M-C. BRCA1 and BRCA2 and the genetics of breast and ovarian cancer. Hum. Mol. Genet., 10: 705-713, 2001
2. Scully, R., Ganescan, S., Brown, M., De Caprio, J. A., Cannistra, S. A., Feunteun, J., Schnitt, S., and Livingston, D. M. Location of BRCA1 in human breast and ovarian cancer cells. Science (Wash. DC), 272: 123-125, 1996
3. Scully, R., Chen, J., Plug, A., Xiao, Y., Weaver, D., Feunteun, J., Ashley, T., and Livingston, D. M. Association of BRCA1 with Rad51 in mitotic and meiotic cells. Cell. 88: 266-275, 1997
4. Zhong, Q., Chen, C. F., Li, S., Chen, Y., Wang, C. C., Xiao, J., Chen, P. L., Sharp, Z. D., and Lee, W. H. Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response. Science (Wash. DC). 285: 747-750, 1999
5. Ruffner, H., and Verma, I. M. BRCA1 is a cell cycle-regulated nuclear phosphoprotein. Proc. Natl. Acad. Sci. USA, 94: 7138-7143, 1997
6. Chen, Y., Farmer, A. A., Chen, C-F., Jones, D. C., Chen, P-L., and Lee, W-H. BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner. Cancer Res., 56: 3168-3172, 1996
7. Ruffner, H., Jiang, W., Craig, A. G., Hunter, T., and Verma, I. M. BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site. Mol. Cell. Biol., 19: 4843-4854, 1999
8. Cortez, D., Wang, Y., Qin, J., and Elledge, S. J. Requirement of ATM-dependent phosphorylation of BRCA1 in the DNA damage response to double-strand breaks. Science (Wash. DC), 286: 1162-1166, 1999
9. Chen, J. Ataxia Telangiectasia-related protein is involved in the phosphorylation of BRCA1 following deoxyribonucleic acid damage. Cancer Res., 60: 5037-5039, 2000
10. Tibbetts, R. S., Cortez, D., Brumbaugh, K. M., Scully, R., Livingston, D., Elledge, S. J., and Abraham, R. T. Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress. Genes Dev., 14: 2989-3002, 2000
11. Thomas, J. E., Smith, M., Tonkinson, J. L., Rubinfeld, B., and Polakis, P. Induction of phosphorylation on BRCA1 during the cell cycle and after DNA damage. Cell Growth Differ., 8: 801-809, 1997
12. Hsu, L-C., and White, R. L. BRCA1 is associated with the centrosome during mitosis. Proc. Natl. Acad. Sci. USA, 95: 12983-12988, 1998
13. Mumby, M. C., and Walter, G. Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol. Rev., 73: 673-699, 1993
14. Shenolikar, S. Protein serine/threonine phosphatases: New avenues for cell regulation. Annu. Rev. Cell Biol., 10: 55-86, 1994
15. Dohadwala, M., Da Cruz e Silva, E. F., Hall, F. L., Williams, R. T., Carbonaro-Hall, D. A., Nairn, A. C., Greengard, P., and Berndt, N. Phosphorylation and inactivation of protein phosphatase I by cyclin-dependent kinases. Proc. Natl. Acad. Sci. USA, 91: 6408-6412, 1994
16. Andreassen, P. R., Lacroix, F. B., Villa-Moruzzi, E., and Margolis, R. L. Differential subcellular localization of protein phosphatase-1 α, γ1, and δ isoforms during both interphase and mitosis in mammalian cells. J. Cell Biol., 141: 1207-1215, 1998
17. Scully, R., Chen, J., Ochs, R. L., Keegan, K., Hoekstra, M., Feunteun, J., and Livingston, D. M. Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. Cell. 90: 425-435, 1997
18. Matsuoka, S., Huang, M., and Elledge, S. J. Linkage of ATM to cell cycle regulation by the Chk2 protein kinase. Science (Wash. DC), 282: 1893-1897, 1998
19. Brown, A. L., Lee, C-H., Schwarz, J. K., Mitiku, N., Piwnica-Worms, H., and Chung, J. H. A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage. Proc. Natl. Acad. Sci. USA, 96: 3745-3750, 1999
20. Chaturvedi, P., Eng, W. K., Zhu, Y., Mattern, M. R., Mishra, R., Hurle, M. R., Zhang, X., Annan, R. S., Lu, Q., Faucette, L. F., Scott, G. F., Li, X., Carr, S. A., Johnson, R. K., Winkler, J. D., and Zhou, B-B. S. Mammalian Chk2 is a downstream effector of the ATM-dependent DNA damage checkpoint pathway. Oncogene, 18: 4047-4054, 1999
21. Lee, J. S., Collins, K. M., Brown, A. L., Lee, C. H., and Chung, J. H. hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage response. Nature (Lond.), 404: 201-204, 2000
22. Hsu, L-C., Doan, T. P., and White, R. L. Identification of a γ-tubulin-binding domain in BRCA1. Cancer Res., 61: 7713-7718, 2001
23. 2-phase checkpoints after ionizing irradiation. Mol. Cell. Biol., 21: 3445-3450, 2001
24. Durfee, T., Becherer, K., Chen, P. L., Yeh, S. H., Yang, Y., Kilburn, A. E., Lee, W. H., and Elledge, S. J. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev., 7: 555-569, 1993
25. Alberts, A. S., Thorburn, A. M., Shenolikar, S., Mumby, M. C., and Feramisco, J. R. Regulation of cell cycle progression and nuclear affinity of the retinoblastoma protein by protein phosphatases. Proc. Natl. Acad. Sci. USA, 90: 388-392, 1993
26. Tamrakar, S., Ludlow, J. W. The carboxyl-terminal region of the retinoblastoma protein binds non-competitively to protein phosphatase type 1α and inhibits catalytic activity. J. Biol. Chem., 275: 27784-27789, 2000