Regulation of p53-MDMX interaction by casein kinase 1 alpha

Molecular and Cellular Biology

Volumn 25, Issue 15, 2005, Pages 6509-6520

  Chen, Lihong ^a   Li, Changgong ^a   Pan, Yu ^a   Chen, Jiandong ^a  

^a H LEE MOFFITT CANCER CENTER AND RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE I; CASEIN KINASE IALPHA; ISOENZYME; PROTEIN MDM2; PROTEIN MDMX; PROTEIN P53; SERINE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

ANIMAL CELL; APOPTOSIS; ARTICLE; CONTROLLED STUDY; DNA DAMAGE; EMBRYO; ENZYME PHOSPHORYLATION; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; IONIZING RADIATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; STRESS; TUMOR SUPPRESSOR GENE; UBIQUITINATION;

ANIMALS; BINDING SITES; CARRIER PROTEINS; CASEIN KINASE IALPHA; HELA CELLS; HUMANS; MICE; NUCLEAR PROTEINS; PHOSPHORYLATION; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-MDM2; RNA INTERFERENCE; SERINE; TUMOR SUPPRESSOR PROTEIN P53;

EID: 22544438112     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.15.6509-6520.2005     Document Type: Article

References (47)

1. Amit, S., A. Hatzubai, Y. Birman, J. S. Andersen, E. Ben-Shushan, M. Mann, Y. Ben-Neriah, and I. Alkalay. 2003. Axin-mediated CKI phosphorylation of beta-catenin at Ser 45: a molecular switch for the Wnt pathway. Genes Dev. 16:1066-1076.
2. Baker, S. J., S. Markowitz, E. R. Fearon, J. K. Willson, and B. Vogelstein. 1990. Suppression of human colorectal carcinoma cell growth by wild-type p53. Science 249:912-915.
3. Blattner, C., T. Hay, D. W. Meek, and D. P. Lane. 2002. Hypophosphorylation of Mdm2 augments p53 stability. Mol. Cell. Biol. 22:6170-6182.
4. Brockman, J. L., S. D. Gross, M. R. Sussman, and R. A. Anderson. 1992. Cell cycle-dependent localization of casein kinase I to mitotic spindles. Proc. Natl. Acad. Sci. USA 89:9454-9458.
5. Chen, J., V. Marechal, and A. J. Levine. 1993. Mapping of the p53 and mdm-2 interaction domains. Mol. Cell. Biol. 13:4107-4114.
6. Chijiwa, T., M. Hagiwara, and H. Hidaka. 1989. A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroisoquinoline-8- sulfonamide, and affinity purification of casein kinase I from bovine testis. J. Biol. Chem. 264:4924-4927.
7. De Graaf, P., N. A. Little, Y. F. Ramos, E. Meulmeester, S. J. Letteboer, and A. G. Jochemsen. 2003. Hdmx protein stability is regulated by the ubiquitin ligase activity of mdm2. J. Biol. Chem. 278:38315-38324.
8. DeMaggio, A. J., R. A. Lindberg, T. Hunter, and M. F. Hoekstra. 1992. The budding yeast HRR25 gene product is a casein kinase I isoform. Proc. Natl. Acad. Sci. USA 89:7008-7012.
9. Desagher, S., A. Osen-Sand, S. Montessuit, E. Magnenat, F. Vilbois, A. Hochmann, L. Journot, B. Antonsson, and J. C. Martinou. 2003. Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol. Cell 8:601-611.
10. Eide, E. J., and D. M. Virshup. 2003. Casein kinase I: another cog in the circadian clockworks. Chronobiol. Int. 18:389-398.
11. Finch, R. A., D. B. Donoviel, D. Potter, M. Shi, A. Fan, D. D. Freed, C. Y. Wang, B. P. Zambrowicz, R. Ramirez-Solis, A. T. Sands, and N. Zhang. 2002. mdmx is a negative regulator of p53 activity in vivo. Cancer Res. 62:3221-3225.
12. Fish, K. J., A. Cegielska, M. E. Getman, G. M. Landes, and D. M. Virshup. 1995. Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family. J. Biol. Chem. 270:14875-14883.
13. Flotow, H., P. R. Graves, A. Q. Wang, C. J. Fiol, R. W. Roeske, and P. J. Roach. 1990. Phosphate groups as substrate determinants for casein kinase I action. J. Biol. Chem. 265:14264-14269.
14. Flotow, H., and P. J. Roach. 1991. Role of acidic residues as substrate determinants for casein kinase I. J. Biol. Chem. 266:3724-3727.
15. Freedman, D. A., C. B. Epstein, J. C. Roth, and A. J. Levine. 1997. A genetic approach to mapping the p53-binding site in the MDM2 protein. Mol. Med. 3:248-259.
16. Gross, S. D., and R. A. Anderson. 1998. Casein kinase I: spatial organization and positioning of a multifunctional protein kinase family. Cell Signal. 10: 699-711.
17. Gross, S. D., J. C. Loijens, and R. A. Anderson. 1999. The casein kinase Ialpha isoform is both physically positioned and functionally competent to regulate multiple events of mRNA metabolism. J. Cell Sci. 112:2647-2656.
18. Gu, J., H. Kawai, L. Nie, H. Kitao, D. Wiederschain, A. G. Jochemsen, J. Parant, G. Lozano, and Z. M. Yuan. 2002. Mutual dependence of MDM2 and MDMX in their functional inactivation of p53. J. Biol. Chem. 277: 19251-19254.
19. Hoekstra, M. F., R. M. Liskay, A. C. Ou, A. J. DeMaggio, D. G. Burbee, and F. Heffron. 1991. HRR25, a putative protein kinase from budding yeast: association with repair of damaged DNA. Science 253:1031-1034.
20. Jackson, M. W., M. S. Lindstrom, and S. J. Berberich. 2002. MdmX binding to ARF affects Mdm2 protein stability and p53 transactivation. J. Biol. Chem. 276:25336-25341.
21. Jin, Y., H. Lee, S. X. Zeng, M. S. Dai, and H. Lu. 2003. MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation. EMBO J. 22:6365-6377.
22. Joazeiro, C. A., and A. M. Weissman. 2002. RING ringer proteins: mediators of ubiquitin ligase activity. Cell 102:549-552.
23. Kafadar, K. A., H. Zhu, M. Snyder, and M. S. Cyert. 2003. Negative regulation of calcineurin signaling by Hrr25p, a yeast homolog of casein kinase I. Genes Dev. 17:2698-2708.
24. Kawai, H., D. Wiederschain, H. Kitao, J. Stuart, K. K. Tsai, and Z. M. Yuan. 2003. DNA damage-induced MDMX degradation is mediated by MDM2. J. Biol. Chem. 278:45946-45953.
25. Knippschild, U., D. M. Milne, L. E. Campbell, A. J. DeMaggio, E. Christenson, M. F. Hoekstra, and D. W. Meek. 1997. p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase- directed drugs. Oncogene 15:1727-1736.
26. Li, C., L. Chen, and J. Chen. 2002. DNA damage induces MDMX nuclear translocation by p53-dependent and -independent mechanisms. Mol. Cell. Biol. 22:7562-7571.
27. Uu, C., Y. Li, M. Semenov, C. Han, G. H. Baeg, Y. Tan, Z. Zhang, X. Lin, and X. He. 2003. Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism. Cell 108:837-847.
28. Midgley, C. A., J. M. Desterro, M. K. Saville, S. Howard, A. Sparks, R. T. Hay, and D. P. Lane. 2001. An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19:2312-2323.
29. Migliorini, D., E. L. Denchi, D. Danovi, A. Jochemsen, M. Capillo, A. Gobbi, K. Helin, P. G. Pelicci, and J. C. Marine. 2002. Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development. Mol. Cell. Biol. 22:5527-5538.
30. Oca Luna, R. M., D. S. Wagner, and G. Lozano. 1995. Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378: 203-206.
31. Pan, Y., and J. Chen. 2003. MDM2 promotes ubiquitination and degradation of MDMX. Mol. Cell. Biol. 23:5113-5121.
32. Parant, J., A. Chavez-Reyes, N. A. Little, W. Yan, V. Reinke, A. G. Jochemsen, and G. Lozano. 2002. Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat. Genet. 29:92-95.
33. Prives, C., and P. A. Hall. 1999. The p53 pathway. J. Pathol. 187:112-126.
34. Ramos, Y. F., R. Stad, J. Attema, L. T. Peltenburg, A. J. van der Eb, and A. G. Jochemsen. 2002. Aberrant expression of HDMX proteins in tumor cells correlates with wild-type p53. Cancer Res. 61:1839-1842.
35. Rowan, B. G., N. Garrison, N. L. Weigel, and B. W. O'Malley. 2000. 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein. Mol. Cell. Biol. 20:8720-8730.
36. Sakaguchi, K., S. Saito, Y. Higashimoto, S. Roy, C. W. Anderson, and E. Appella. 2000. Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding. J. Biol. Chem. 275:9278-9283.
37. Santos, J. A., E. Logarinho, C. Tapia, C. C. Allende, J. E. Allende, and C. E. Sunkel. 1996. The casein kinase 1 alpha gene of Drosophila melanogaster is developmentally regulated and the kinase activity of the protein induced by DNA damage. J. Cell Sci. 109:1847-1856.
38. Sharp, D. A., S. A. Kratowicz, M. J. Sank, and D. L. George. 1999. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274:38189-38196.
39. Shvarts, A., W. T. Steegenga, N. Riteco, T. van Larr, P. Dekker, M. Bazuine, R. C. A. van Ham, W. van der Houven van Oordt, G. Hateboer, A. J. van der Eb, and A. G. Jochemsen. 1996. MDMX: a novel p53-binding protein with some functional properties of MDM2. EMBO J. 15:5349-5357.
40. Songyang, Z., K. P. Lu, Y. T. Kwon, L. H. Tsai, O. Filhol, C. Cochet, D. A. Brickey, T. R. Soderling, C. Bartleson, D. J. Graves, A. J. DeMaggio, M. F. Hoekstra, J. Blenis, T. Hunter, and L. C. Cantley. 1996. A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. Mol. Cell. Biol. 16:6486-6493.
41. Stad, R., N. A. Little, D. P. Xirodimas, R. Frenk, A. J. van der Eb, D. P. Lane, M. K. Saville, and A. G. Jochemsen. 2001. Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms. EMBO Rep. 2:1029-1034.
42. Tzivion, G., and J. Avruch. 2002. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277:3061-3064.
43. Tzivion, G., Y. H. Shen, and J. Zhu. 2001. 14-3-3 proteins: bringing new definitions to scaffolding. Oncogene 20:6331-6338.
44. Vousden, K. H. 2000. p53: death star. Cell 103:691-694.
45. Winter, M., D. Milne, S. Dias, R. Kulikov, U. Knippschild, C. Blattner, and D. Meek. 2004. Protein kinase CK1delta phosphorylates key sites in the acidic domain of murine double-minute clone 2 protein (MDM2) that regulate p53 turnover. Biochemistry 43:16356-16364.
46. Zhang, Y., and Y. Xiong. 2001. Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ. 12:175-186.
47. Zhu, J., F. Shibasaki, R. Price, J. C. Guillemot, T. Yano, V. Dotsch, G. Wagner, P. Ferrara, and F. McKeon. 1998. Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase I and MEKK1. Cell 93:851-861.