Mouse Wee1 Gene Is Repressed by Krüppel-Like Factor 3 (KLF3) via Interaction with Multiple Upstream Elements

Gene

Volumn 492, Issue 2, 2012, Pages 361-367

  Kitamura, Takuya ^a   Suzuki, Hidefumi ^a   Tamura, Taka aki ^a  

^a CHIBA UNIVERSITY   (Japan)

Author keywords

CACCC box; KLF3; TLP; Transcriptional repression; Wee1

Indexed keywords

KRUPPEL LIKE FACTOR; KRUPPEL LIKE FACTOR 3; MESSENGER RNA; PROTEIN KINASE; TATA BINDING PROTEIN RELATED FACTOR; UNCLASSIFIED DRUG; WEE1 PROTEIN KINASE;

ARTICLE; BINDING SITE; CELL CYCLE G2 PHASE; CELL CYCLE M PHASE; CONTROLLED STUDY; DOWN REGULATION; GENE OVEREXPRESSION; GENE REPRESSION; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN PROTEIN INTERACTION; REPORTER GENE;

ANIMALS; BINDING SITES; CELL CYCLE PROTEINS; GENE EXPRESSION; GENE EXPRESSION REGULATION; KRUPPEL-LIKE TRANSCRIPTION FACTORS; MICE; NUCLEAR PROTEINS; PROMOTER REGIONS, GENETIC; PROTEIN-TYROSINE KINASES; REGULATORY ELEMENTS, TRANSCRIPTIONAL;

EID: 84655176710     PISSN: 03781119     EISSN: 18790038     Source Type: Journal    
DOI: 10.1016/j.gene.2011.11.016     Document Type: Article

References (30)

1. Banerjee S.S., et al. The Kruppel-like factor KLF2 inhibits peroxisome proliferator-activated receptor-gamma expression and adipogenesis. J. Biol. Chem. 2003, 278:2581-2584.
2. Crossley M., et al. Isolation and characterization of the cDNA encoding BKLF/TEF-2, a major CACCC-box-binding protein in erythroid cells and selected other cells. Mol. Cell. Biol. 1996, 16:1695-1705.
3. Eaton S.A., et al. A network of Kruppel-like Factors (Klfs). Klf8 is repressed by Klf3 and activated by Klf1 in vivo. J. Biol. Chem. 2008, 283:26937-26947.
4. Gould K.L., Nurse P. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 1989, 342:39-45.
5. Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988, 241:42-52.
6. Himeda C.L., Ranish J.A., Pearson R.C., Crossley M., Hauschka S.D. KLF3 regulates muscle-specific gene expression and synergizes with serum response factor on KLF binding sites. Mol. Cell. Biol. 2010, 30:3430-3443.
7. Honda R., Tanaka H., Ohba Y., Yasuda H. Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation. Chromosome Res. 1995, 3:300-308.
8. Kaczynski J., Cook T., Urrutia R. Sp1- and Kruppel-like transcription factors. Genome Biol. 2003, 4:206.
9. Kawasaki H., et al. c-Fos/activator protein-1 transactivates wee1 kinase at G(1)/S to inhibit premature mitosis in antigen-specific Th1 cells. EMBO J. 2001, 20:4618-4627.
10. Matsuo T., et al. Control mechanism of the circadian clock for timing of cell division in vivo. Science 2003, 302:255-259.
11. McGowan C.H., Russell P. Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15. EMBO J. 1993, 12:75-85.
12. Nakadai T., Shimada M., Shima D., Handa H., Tamura T.A. Specific interaction with transcription factor IIA and localization of the mammalian TATA-binding protein-like protein (TLP/TRF2/TLF). J. Biol. Chem. 2004, 279:7447-7455.
13. Nakajo N., et al. Absence of Wee1 ensures the meiotic cell cycle in Xenopus oocytes. Genes Dev. 2000, 14:328-338.
14. Ohbayashi T., Makino Y., Tamura T. Identification of a mouse TBP-like protein (TLP) distantly related to the Drosophila TBP-related factor. Nucleic Acids Res. 1999, 27:750-755.
15. Parker L.L., Atherton-Fessler S., Piwnica-Worms H. p107wee1 is a dual-specificity kinase that phosphorylates p34cdc2 on tyrosine 15. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:2917-2921.
16. Russell P., Nurse P. Negative regulation of mitosis by wee1+, a gene encoding a protein kinase homolog. Cell 1987, 49:559-567.
17. SenBanerjee S., et al. KLF2 Is a novel transcriptional regulator of endothelial proinflammatory activation. J. Exp. Med. 2004, 199:1305-1315.
18. Shimada M., Nakadai T., Tamura T.A. TATA-binding protein-like protein (TLP/TRF2/TLF) negatively regulates cell cycle progression and is required for the stress-mediated G(2) checkpoint. Mol. Cell. Biol. 2003, 23:4107-4120.
19. Shiraishi S., et al. TBP-interacting protein 120B (TIP120B)/cullin-associated and neddylation-dissociated 2 (CAND2) Inhibits SCF-dependent ubiquitination of myogenin and accelerates myogenic differentiation. J. Biol. Chem. 2007, 282:9017-9018.
20. Solomon M.J., Lee T., Kirschner M.W. Role of phosphorylation in p34cdc2 activation: identification of an activating kinase. Mol. Biol. Cell 1992, 3:13-27.
21. Suenaga Y., et al. TATA-binding Protein (TBP)-like Protein Is Engaged in Etoposide-induced Apoptosis through Transcriptional Activation of Human TAp63 Gene. J. Biol. Chem. 2009, 284:35433-35440.
22. Tanaka Y., et al. Transcriptional repression of the mouse wee1 gene by TBP-related factor 2. Biochem. Biophys. Res. Commun. 2007, 352:21-28.
23. Turner J., Crossley M. Cloning and characterization of mCtBP2, a co-repressor that associates with basic Kruppel-like factor and other mammalian transcriptional regulators. EMBO J. 1998, 17:5129-5140.
24. van Vliet J., et al. Human KLF17 is a new member of the Sp/KLF family of transcription factors. Genomics 2006, 87:474-482.
25. Wang F., et al. Transcriptional repression of WEE1 by Kruppel-like factor 2 is involved in DNA damage-induced apoptosis. Oncogene 2005, 24:3875-3885.
26. Watanabe N., Broome M., Hunter T. Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle. EMBO J. 1995, 14:1878-1891.
27. Watanabe N., et al. Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:11663-11668.
28. Wu J., Lingrel J.B. KLF2 inhibits Jurkat T leukemia cell growth via upregulation of cyclin-dependent kinase inhibitor p21WAF1/CIP1. Oncogene 2004, 23:8088-8096.
29. Yarden R.I., Pardo-Reoyo S., Sgagias M., Cowan K.H., Brody L.C. BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage. Nat. Genet. 2002, 30:285-289.
30. Zhao L.J., Kuppuswamy M., Vijayalingam S., Chinnadurai G. Interaction of ZEB and histone deacetylase with the PLDLS-binding cleft region of monomeric C-terminal binding protein 2. BMC Mol. Biol. 2009, 10:89.