Identification of a putative nuclear export signal motif in human NANOG homeobox domain

Biochemical and Biophysical Research Communications

Volumn 421, Issue 3, 2012, Pages 484-489

  Park, Sung Won ^a   Do, Hyun Jin ^a   Huh, Sun Hyung ^a   Sung, Boreum ^a   Uhm, Sang Jun ^b   Song, Hyuk ^c   Kim, Nam Hyung ^d   Kim, Jae Hwan ^a  

^a CHA University   (South Korea)

^b Sangji Youngseo College   (South Korea)

^c Konkuk University   (South Korea)

^d Chungbuk National University   (South Korea)

Author keywords

Homeobox domain; Leucine rich motif; NANOG; Nuclear export signal

Indexed keywords

ENHANCED GREEN FLUORESCENT PROTEIN; HOMEODOMAIN PROTEIN; TRANSCRIPTION FACTOR NANOG;

ARTICLE; CELL NUCLEUS; CELL STRAIN COS7; CONFOCAL MICROSCOPY; CYTOPLASM; HUMAN; HUMAN CELL; MUTAGENESIS; NUCLEAR EXPORT SIGNAL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; WESTERN BLOTTING;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CELL NUCLEUS; CERCOPITHECUS AETHIOPS; COS CELLS; HOMEODOMAIN PROTEINS; HUMANS; KARYOPHERINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEAR EXPORT SIGNALS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SEQUENCE ANALYSIS, DNA;

EID: 84860693853     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.025     Document Type: Article

References (39)

1. Chambers I., Colby D., Robertson M., et al. Functional expression cloning of Nanog, a pluripotency sustaining factor in embryonic stem cells. Cell 2003, 113:643-655.
2. Mitsui K., Tokuzawa Y., Itoh H., et al. The homeoprotein Nanog is required for maintenance of pluripotency in mouse epiblast and ES cells. Cell 2003, 113:631-642.
3. Theunissen T.W., Silva J.C. Switching on pluripotency: a perspective on the biological requirement of Nanog. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 2011, 366:2222-2229.
4. Wang J., Levasseur D.N., Orkin S.H. Requirement of Nanog dimerization for stem cell self-renewal and pluripotency. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:6326-6331.
5. Chang D.F., Tsai S.C., Wang X.C., et al. Molecular characterization of the human NANOG protein. Stem Cells 2009, 27:812-821.
6. Jeter C.R., Badeaux M., Choy G., et al. Functional evidence that the self-renewal gene NANOG regulates human tumor development. Stem Cells 2009, 27:993-1005.
7. Hoei-Hansen C.E. Application of stem cell markers in search for neoplastic germ cells in dysgenetic gonads, extragonadal tumours, and in semen of infertile men. Cancer Treat. Rev. 2008, 34:348-367.
8. Ezeh U.I., Turek P.J., Reijo R.A., Clark A.T. Human embryonic stem cell genes OCT4, NANOG, STELLAR, and GDF3 are expressed in both seminoma and breast carcinoma. Cancer 2005, 104:2255-2265.
9. Ye F., Zhou C., Cheng Q., et al. Stem-cell-abundant proteins Nanog, Nucleostemin and Musashi1 are highly expressed in malignant cervical epithelial cells. BMC Cancer 2008, 8:108.
10. Chiou S.H., Yu C.C., Huang C.Y., et al. Positive correlations of Oct-4 and Nanog in oral cancer stem-like cells and high-grade oral squamous cell carcinoma. Clin. Cancer Res. 2008, 14:4085-4095.
11. Bussolati B., Bruno S., Grange C., et al. Identification of a tumor-initiating stem cell population in human renal carcinomas. FASEB J. 2008, 22:3696-3705.
12. Chiou S.H., Wang M.L., Chou Y.T., et al. Coexpression of Oct4 and Nanog enhances malignancy in lung adenocarcinoma by inducing cancer stem cell-like properties and epithelial-mesenchymal transdifferentiation. Cancer Res. 2010, 70:10433-10444.
13. Wen J., Park J.Y., Park K.H., et al. Oct4 and Nanog expression is associated with early stages of pancreatic carcinogenesis. Pancreas 2010, 39:622-626.
14. Pan Y., Jiao J., Zhou C., et al. Nanog is highly expressed in ovarian serous cystadenocarcinoma and correlated with clinical stage and pathological grade. Pathobiology 2010, 77:283-288.
15. Guo Y., Liu S., Wang P., et al. Expression profile of embryonic stem cell-associated genes Oct4, Sox2 and Nanog in human gliomas. Histopathology 2011, 59:763-775.
16. Zhang J., Wang X., Chen B., et al. Expression of Nanog gene promotes NIH3T3 cell proliferation. Biochem. Biophys. Res. Commun. 2005, 338:1098-1102.
17. Liu T.M., Wu Y.N., Guo X.M., et al. Effects of ectopic Nanog and Oct4 overexpression on mesenchymal stem cells. Stem Cells Dev. 2009, 18:1013-1022.
18. Lin Y.L., Han Z.B., Xiong F.Y., et al. Malignant transformation of 293 cells induced by ectopicexpression of human Nanog. Mol. Cell. Biochem. 2011, 351:109-116.
19. Ambady S., Malcuit C., Kashpur O., et al. Expression of NANOG and NANOGP8 in a variety of undifferentiated and differentiated human cells. Int. J. Dev. Biol. 2010, 54:1743-1754.
20. Ishiguro T., Sato A., Ohata H., et al. Differential expression of nanog1 and nanogp8 in colon cancer cells. Biochem. Biophys. Res. Commun. 2012, 418:199-204.
21. Görlich D., Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell. Dev. Biol. 1999, 15:607-660.
22. Schwoebel E.D., Moore M.S. The control of gene expression by regulated nuclear transport. Essays Biochem. 2000, 36:105-113.
23. Jans D.A., Xiao C.Y., Lam M.H. Nuclear targeting signal recognition: a key control point in nuclear transport?. Bioessays 2000, 22:532-544.
24. Fornerod M., Ohno M., Yoshida M., Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997, 90:1051-1060.
25. Oh J.H., Do H.J., Yang H.M., et al. Identification of a putative transactivation domain in human Nanog. Exp. Mol. Med. 2005, 37:250-254.
26. Do H.J., Lee W.Y., Lim H.Y., et al. Two potent transactivation domains in the C-terminal region of human NANOG mediate transcriptional activation in human embryonic carcinoma cells. J. Cell. Biochem. 2009, 106:1079-1089.
27. McKinnon C.M., Docherty K. Pancreatic duodenal homeobox-1, PDX-1, a major regulator of beta cell identity and function. Diabetologia 2001, 44:1203-1214.
28. Chi N., Epstein J.A. Getting your Pax straight: Pax proteins in development and disease. Trends Genet. 2002, 18:41-47.
29. Theunissen T.W., Costa Y., Radzisheuskaya A., et al. Reprogramming capacity of Nanog is functionally conserved in vertebrates and resides in a unique homeodomain. Development 2011, 138:4853-4865.
30. Do H.J., Lim H.Y., Kim J.H., et al. An intact homeobox domain is required for complete nuclear localization of human Nanog. Biochem. Biophys. Res. Commun. 2007, 353:770-775.
31. Baranek C., Sock E., Wegner M. The POU protein Oct-6 is a nucleocytoplasmic shuttling protein. Nucleic Acids Res. 2005, 33:6277-6286.
32. Ilia M., Bazigou E., Price J. Expression of the POU domain transcription factor, Oct-6, is attenuated in the adult mouse telencephalon, but increased by neurotoxic damage. Exp. Neurol. 2003, 181:159-169.
33. Andrews N.C., Faller D.V. A rapid micropreparation technique for extraction of DNA-binding proteins from limiting numbers of mammalian cells. Nucleic Acids Res. 1991, 19:2499.
34. Cerutti A., Maillard P., Minisini R., et al. Identification of a functional, CRM-1-dependent nuclear export signal in hepatitis C virus core protein. PLoS One 2011, 6:e25854.
35. la Cour T., Kiemer L., Molgaard A., et al. Analysis and prediction of leucine-rich nuclear export signals. Protein Eng. Des. Sel. 2004, 17:527-536.
36. Rehberg S., Lischka P., Glaser G., et al. Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is crucial for Sox10-mediated transactivation. Mol. Cell. Biol. 2002, 22:5826-5834.
37. Dong X., Biswas A., Süel K.E., et al. Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature 2009, 458:1136-1141.
38. Xu D., Farmer A., Chook Y.M. Recognition of nuclear targeting signals by Karyopherin-β proteins. Curr. Opin. Struct. Biol. 2010, 20:782-790.
39. Ye W., Lin W., Tartakoff A.M., Tao T. Karyopherins in nuclear transport of homeodomain proteins during development. Biochim. Biophys. Acta 1813, 2011:1654-1662.