Selenoprotein W promotes cell cycle recovery from G2 arrest through the activation of CDC25B

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1823, Issue 12, 2012, Pages 2217-2226

  Park, Yong Hwan ^a   Jeon, Yeong Ha ^a   Kim, Ick Young ^a  

^a Korea University   (South Korea)

Author keywords

14 3 3; CDC25B; Cdk1; Cell cycle; G2 arrest; Selenoprotein W

Indexed keywords

CDC25B PROTEIN; CYCLIN DEPENDENT KINASE 1; DNA; PHOSPHATASE; SELENOPROTEIN W; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL CYCLE PROGRESSION; CONTROLLED STUDY; DNA DAMAGE; EMBRYO; ENZYME ACTIVATION; ENZYME INACTIVATION; ENZYME PHOSPHORYLATION; G2 PHASE CELL CYCLE CHECKPOINT; GENE SILENCING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION;

14-3-3 PROTEINS; ANIMALS; APOPTOSIS; BLOTTING, WESTERN; CDC25 PHOSPHATASES; CELL PROLIFERATION; COLONY-FORMING UNITS ASSAY; FLOW CYTOMETRY; G2 PHASE CELL CYCLE CHECKPOINTS; HUMANS; IMMUNOPRECIPITATION; MICE; NIH 3T3 CELLS; PROTEIN KINASES; REAL-TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; RNA, SMALL INTERFERING; SELENOPROTEIN W;

EID: 84867379834     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.09.001     Document Type: Article

References (52)

1. Papp L.V., Lu J., Holmgren A., Khanna K.K. From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid. Redox Signal. 2007, 9:775-806.
2. Kryukov G.V., Castellano S., Novoselov S.V., Lobanov A.V., Zehtab O., Guigo R., Gladyshev V.N. Characterization of mammalian selenoproteomes. Science 2003, 300:1439-1443.
3. Lu J., Holmgren A. Selenoproteins. J. Biol. Chem. 2009, 284:723-727.
4. Jeong D.W., Kim E.H., Kim T.S., Chung Y.W., Kim H., Kim I.Y. Different distributions of selenoprotein W and thioredoxin during postnatal brain development and embryogenesis. Mol. Cells 2004, 17:156-159.
5. Vendeland S.C., Beilstein M.A., Chen C.L., Jensen O.N., Barofsky E., Whanger P.D. Purification and properties of selenoprotein W from rat muscle. J. Biol. Chem. 1993, 268:17103-17107.
6. Jeong D., Kim T.S., Chung Y.W., Lee B.J., Kim I.Y. Selenoprotein W is a glutathione-dependent antioxidant in vivo. FEBS Lett. 2002, 517:225-228.
7. Chung Y.W., Jeong D., Noh O.J., Park Y.H., Kang S.I., Lee M.G., Lee T.H., Yim M.B., Kim I.Y. Antioxidative role of selenoprotein W in oxidant-induced mouse embryonic neuronal cell death. Mol. Cells 2009, 27:609-613.
8. Musiani F., Ciurli S., Dikiy A. Interaction of selenoprotein W with 14-3-3 proteins: a computational approach. J. Proteome Res. 2011, 10:968-976.
9. Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A., Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N. SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family. Biochemistry 2007, 46:6871-6882.
10. Aachmann F.L., Fomenko D.E., Soragni A., Gladyshev V.N., Dikiy A. Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins. J. Biol. Chem. 2007, 282:37036-37044.
11. Hawkes W.C., Wang T.T., Alkan Z., Richter B.D., Dawson K. Selenoprotein W modulates control of cell cycle entry. Biol. Trace Elem. Res. 2009, 131:229-244.
12. Lew D.J., Kornbluth S. Regulatory roles of cyclin dependent kinase phosphorylation in cell cycle control. Curr. Opin. Cell Biol. 1996, 8:795-804.
13. Coleman T.R., Dunphy W.G. Cdc2 regulatory factors. Curr. Opin. Cell Biol. 1994, 6:877-882.
14. Kastan M.B., Bartek J. Cell-cycle checkpoints and cancer. Nature 2004, 432:316-323.
15. O'Connell M.J., Walworth N.C., Carr A.M. The G2-phase DNA-damage checkpoint. Trends Cell Biol. 2000, 10:296-303.
16. Bartek J., Lukas J. DNA damage checkpoints: from initiation to recovery or adaptation. Curr. Opin. Cell Biol. 2007, 19:238-245.
17. van Vugt M.A., Bras A., Medema R.H. Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol. Cell 2004, 15:799-811.
18. Buhrman G., Parker B., Sohn J., Rudolph J., Mattos C. Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond. Biochemistry 2005, 44:5307-5316.
19. Giles N., Forrest A., Gabrielli B. 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity. J. Biol. Chem. 2003, 278:28580-28587.
20. Forrest A., Gabrielli B. Cdc25B activity is regulated by 14-3-3. Oncogene 2001, 20:4393-4401.
21. Savitsky P.A., Finkel T. Redox regulation of Cdc25C. J. Biol. Chem. 2002, 277:20535-20540.
22. Papp L.V., Lu J., Striebel F., Kennedy D., Holmgren A., Khanna K.K. The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function. Mol. Cell. Biol. 2006, 26:4895-4910.
23. Vazquez-Novelle M.D., Mailand N., Ovejero S., Bueno A., Sacristan M.P. Human Cdc14A phosphatase modulates the G2/M transition through Cdc25A and Cdc25B. J. Biol. Chem. 2010, 285:40544-40553.
24. Noh O.J., Park Y.H., Chung Y.W., Kim I.Y. Transcriptional regulation of selenoprotein W by MyoD during early skeletal muscle differentiation. J. Biol. Chem. 2010, 285:40496-40507.
25. Borlongan C.V., Yamamoto M., Takei N., Kumazaki M., Ungsuparkorn C., Hida H., Sanberg P.R., Nishino H. Glial cell survival is enhanced during melatonin-induced neuroprotection against cerebral ischemia. FASEB J. 2000, 14:1307-1317.
26. Weng L.P., Smith W.M., Dahia P.L., Ziebold U., Gil E., Lees J.A., Eng C. PTEN suppresses breast cancer cell growth by phosphatase activity-dependent G1 arrest followed by cell death. Cancer Res. 1999, 59:5808-5814.
27. Zheng L., Ren J.Q., Li H., Kong Z.L., Zhu H.G. Downregulation of wild-type p53 protein by HER-2/neu mediated PI3K pathway activation in human breast cancer cells: its effect on cell proliferation and implication for therapy. Cell Res. 2004, 14:497-506.
28. Gould K.L., Nurse P. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 1989, 342:39-45.
29. Jin P., Hardy S., Morgan D.O. Nuclear localization of cyclin B1 controls mitotic entry after DNA damage. J. Cell Biol. 1998, 141:875-885.
30. Yang J., Song H., Walsh S., Bardes E.S., Kornbluth S. Combinatorial control of cyclin B1 nuclear trafficking through phosphorylation at multiple sites. J. Biol. Chem. 2001, 276:3604-3609.
31. McGowan C.H., Russell P. Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15. EMBO J. 1993, 12:75-85.
32. Wang Y., Jacobs C., Hook K.E., Duan H., Booher R.N., Sun Y. Binding of 14-3-3beta to the carboxyl terminus of Wee1 increases Wee1 stability, kinase activity, and G2-M cell population. Cell Growth Differ. 2000, 11:211-219.
33. Lindqvist A., Kallstrom H., Lundgren A., Barsoum E., Rosenthal C.K. Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1-Cdk1 at the centrosome. J. Cell Biol. 2005, 171:35-45.
34. Varmeh S., Manfredi J.J. Inappropriate activation of cyclin-dependent kinases by the phosphatase Cdc25b results in premature mitotic entry and triggers a p53-dependent checkpoint. J. Biol. Chem. 2009, 284:9475-9488.
35. Woo E.S., Rice R.L., Lazo J.S. Cell cycle dependent subcellular distribution of Cdc25B subtypes. Oncogene 1999, 18:2770-2776.
36. Davezac N., Baldin V., Gabrielli B., Forrest A., Theis-Febvre N., Yashida M., Ducommun B. Regulation of CDC25B phosphatases subcellular localization. Oncogene 2000, 19:2179-2185.
37. Huang H.L., Fang L.W., Lu S.P., Chou C.K., Luh T.Y., Lai M.Z. DNA-damaging reagents induce apoptosis through reactive oxygen species-dependent Fas aggregation. Oncogene 2003, 22:8168-8177.
38. Xiao-Long W., Chuan-Ping Y., Kai X., Ou-Jv Q. Selenoprotein W depletion in vitro might indicate that its main function is not as an antioxidative enzyme. Biochemistry (Mosc.) 2010, 75:201-207.
39. Goodarzi A.A., Noon A.T., Deckbar D., Ziv Y., Shiloh Y., Lobrich M., Jeggo P.A. ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin. Mol. Cell 2008, 31:167-177.
40. Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 2003, 423:769-773.
41. Leslie N.R., Lindsay Y., Ross S.H., Downes C.P. Redox regulation of phosphatase function. Biochem. Soc. Trans. 2004, 32:1018-1020.
42. Lee S.R., Yang K.S., Kwon J., Lee C., Jeong W., Rhee S.G. Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 2002, 277:20336-20342.
43. Kim H.Y., Gladyshev V.N. Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases. PLoS Biol. 2005, 3:e375.
44. Lee S.R., Bar-Noy S., Kwon J., Levine R.L., Stadtman T.C., Rhee S.G. Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:2521-2526.
45. Grogan T.M., Fenoglio-Prieser C., Zeheb R., Bellamy W., Frutiger Y., Vela E., Stemmerman G., Macdonald J., Richter L., Gallegos A., Powis G. Thioredoxin, a putative oncogene product, is overexpressed in gastric carcinoma and associated with increased proliferation and increased cell survival. Hum. Pathol. 2000, 31:475-481.
46. Yoo M.H., Xu X.M., Carlson B.A., Gladyshev V.N., Hatfield D.L. Thioredoxin reductase 1 deficiency reverses tumor phenotype and tumorigenicity of lung carcinoma cells. J. Biol. Chem. 2006, 281:13005-13008.
47. Boutros R., Lobjois V., Ducommun B. CDC25 phosphatases in cancer cells: key players? Good targets?. Nat. Rev. Cancer 2007, 7:495-507.
48. Kristjansdottir K., Rudolph J. Cdc25 phosphatases and cancer. Chem. Biol. 2004, 11:1043-1051.
49. Hawkes W.C., Alkan Z. Delayed cell cycle progression in selenoprotein W-depleted cells is regulated by a mitogen-activated protein kinase kinase 4-p38/c-Jun NH2-terminal kinase-p53 pathway. J. Biol. Chem. 2012, 287:27371-27379.
50. Brisson M., Nguyen T., Wipf P., Joo B., Day B.W., Skoko J.S., Schreiber E.M., Foster C., Bansal P., Lazo J.S. Redox regulation of Cdc25B by cell-active quinolinediones. Mol. Pharmacol. 2005, 68:1810-1820.
51. Jullien D., Bugler B., Dozier C., Cazales M., Ducommun B. Identification of N-terminally truncated stable nuclear isoforms of CDC25B that are specifically involved in G2/M checkpoint recovery. Cancer Res. 2011, 71:1968-1977.
52. Ito Y., Yoshida H., Uruno T., Takamura Y., Miya A., Kuma K., Miyauchi A. Expression of cdc25A and cdc25B phosphatase in breast carcinoma. Breast Cancer 2004, 11:295-300.