The role of O-linked GlcNAc modification on the glucose response of ChREBP

Biochemical and Biophysical Research Communications

Volumn 402, Issue 4, 2010, Pages 784-789

  Sakiyama, Haruhiko ^a   Fujiwara, Noriko ^a   Noguchi, Takahiro ^a   Eguchi, Hironobu ^a   Yoshihara, Daisaku ^a   Uyeda, Kosaku ^b   Suzuki, Keiichiro ^a  

^a HYOGO COLLEGE OF MEDICINE   (Japan)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

ChREBP; Mlx; O GlcNAc; Subcellular localization; Transcription factor

Indexed keywords

6 DIAZO 5 OXONORLEUCINE; BASIC LEUCINE ZIPPER TRANSCRIPTION FACTOR; BINDING PROTEIN; CARBOHYDRATE RESPONSE ELEMENT BINDING PROTEIN; CELL PROTEIN; GLYCOSYLTRANSFERASE INHIBITOR; HEXOSAMINE; MAX LIKE PROTEIN X; N ACETYLGLUCOSAMINE; O (2 ACETAMIDO 2 DEOXY DEXTRO GLUCOPYANOSYLIDENE)AMINO N PHENYLCARBAMATE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

ARTICLE; CELL NUCLEUS; CELL STRAIN HEK293; CELLULAR DISTRIBUTION; CONTROLLED STUDY; EMBRYO; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN LOCALIZATION; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

ACETYLGLUCOSAMINE; BASIC HELIX-LOOP-HELIX LEUCINE ZIPPER TRANSCRIPTION FACTORS; BETA-N-ACETYLHEXOSAMINIDASES; CELL LINE; GLUCOSE; GLYCOSYLATION; HUMANS; MUTATION; OXIMES; PHENYLCARBAMATES; TRANSCRIPTION, GENETIC;

EID: 78649443736     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.10.113     Document Type: Article

References (30)

1. Brown M.S., Goldstein J.L. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 1997, 89:331-340.
2. Foretz M., Guichard C., Ferre P., Foufelle F. Sterol regulatory element binding protein-1c is a major mediator of insulin action on the hepatic expression of glucokinase and lipogenesis-related genes. Proc. Natl. Acad. Sci. USA 1999, 96:12737-12742.
3. Osborne T.F. Sterol regulatory element-binding proteins (SREBPs): key regulators of nutritional homeostasis and insulin action. J. Biol. Chem. 2000, 275:32379-32382.
4. Yamashita H., Takenoshita M., Sakurai M., Bruick R.K., Henzel W.J., Shillinglaw W., Arnot D., Uyeda K. A glucose-responsive transcription factor that regulates carbohydrate metabolism in the liver. Proc. Natl. Acad. Sci. USA 2001, 98:9116-9121.
5. Iizuka K., Bruick R.K., Liang G., Horton J.D., Uyeda K. Deficiency of carbohydrate response element-binding protein (ChREBP) reduces lipogenesis as well as glycolysis. Proc. Natl. Acad. Sci. USA 2004, 101:7281-7286.
6. Cairo S., Merla G., Urbinati F., Ballabio A., Reymond A. WBSCR14, a gene mapping to the Williams-Beuren syndrome deleted region, is a new member of the Mlx transcription factor network. Hum. Mol. Genet. 2001, 10:617-627.
7. Ma L., Tsatsos N.G., Towle H.C. Direct role of ChREBP. Mlx in regulating hepatic glucose-responsive genes. J. Biol. Chem. 2005, 280:12019-12027.
8. Stoeckman A.K., Ma L., Towle H.C. Mlx is the functional heteromeric partner of the carbohydrate response element-binding protein in glucose regulation of lipogenic enzyme genes. J. Biol. Chem. 2004, 279:15662-15669.
9. Ishii S., Iizuka K., Miller B.C., Uyeda K. Carbohydrate response element binding protein directly promotes lipogenic enzyme gene transcription. Proc. Natl. Acad. Sci. USA 2004, 101:15597-15602.
10. Sakiyama H., Wynn R.M., Lee W.R., Fukasawa M., Mizuguchi H., Gardner K.H., Repa J.J., Uyeda K. Regulation of nuclear import/export of carbohydrate response element-binding protein (ChREBP): interaction of an alpha-helix of ChREBP with the 14-3-3 proteins and regulation by phosphorylation. J. Biol. Chem. 2008, 283:24899-24908.
11. Kabashima T., Kawaguchi T., Wadzinski B.E., Uyeda K. Xylulose 5-phosphate mediates glucose-induced lipogenesis by xylulose 5-phosphate-activated protein phosphatase in rat liver. Proc. Natl. Acad. Sci. USA 2003, 100:5107-5112.
12. Kawaguchi T., Takenoshita M., Kabashima T., Uyeda K. Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein. Proc. Natl. Acad. Sci. USA 2001, 98:13710-13715.
13. Billin A.N., Eilers A.L., Queva C., Ayer D.E. Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. J. Biol. Chem. 1999, 274:36344-36350.
14. Meroni G., Cairo S., Merla G., Messali S., Brent R., Ballabio A., Reymond A. Mlx, a new Max-like bHLHZip family member: the center stage of a novel transcription factors regulatory pathway?. Oncogene 2000, 19:3266-3277.
15. Luscher B. Function and regulation of the transcription factors of the Myc/Max/Mad network. Gene 2001, 277:1-14.
16. Ma L., Robinson L.N., Towle H.C. ChREBP*Mlx is the principal mediator of glucose-induced gene expression in the liver. J. Biol. Chem. 2006, 281:28721-28730.
17. Vosseller K., Sakabe K., Wells L., Hart G.W. Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification. Curr. Opin. Chem. Biol. 2002, 6:851-857.
18. Wells L., Vosseller K., Hart G.W. Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc. Science 2001, 291:2376-2378.
19. Hanover J.A. Glycan-dependent signaling: O-linked N-acetylglucosamine. FASEB J. 2001, 15:1865-1876.
20. Comer F.I., Hart G.W. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and O-phosphate. J. Biol. Chem. 2000, 275:29179-29182.
21. Hart G.W. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 1997, 66:315-335.
22. Comer F.I., Hart G.W. O-GlcNAc and the control of gene expression. Biochim. Biophys. Acta 1999, 1473:161-171.
23. Naya F.J., Stellrecht C.M., Tsai M.J. Tissue-specific regulation of the insulin gene by a novel basic helix-loop-helix transcription factor. Genes Dev. 1995, 9:1009-1019.
24. Apfel R., Benbrook D., Lernhardt E., Ortiz M.A., Salbert G., Pfahl M. A novel orphan receptor specific for a subset of thyroid hormone-responsive elements and its interaction with the retinoid/thyroid hormone receptor subfamily. Mol. Cell. Biol. 1994, 14:7025-7035.
25. Teboul M., Enmark E., Li Q., Wikstrom A.C., Pelto-Huikko M., Gustafsson J.A. OR-1, a member of the nuclear receptor superfamily that interacts with the 9-cis-retinoic acid receptor. Proc. Natl. Acad. Sci. USA 1995, 92:2096-2100.
26. Andrali S.S., Qian Q., Ozcan S. Glucose mediates the translocation of NeuroD1 by O-linked glycosylation. J. Biol. Chem. 2007, 282:15589-15596.
27. Anthonisen E.H., Berven L., Holm S., Nygard M., Nebb H.I., Gronning-Wang L.M. Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose. J. Biol. Chem. 2010, 285:1607-1615.
28. Ma L., Sham Y.Y., Walters K.J., Towle H.C. A critical role for the loop region of the basic helix-loop-helix/leucine zipper protein Mlx in DNA binding and glucose-regulated transcription. Nucleic Acids Res. 2007, 35:35-44.
29. Kamemura K., Hayes B.K., Comer F.I., Hart G.W. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: alternative glycosylation/phosphorylation of THR-58, a known mutational hot spot of c-Myc in lymphomas, is regulated by mitogens. J. Biol. Chem. 2002, 277:19229-19235.
30. Dauphinee S.M., Ma M., Too C.K. Role of O-linked beta-N-acetylglucosamine modification in the subcellular distribution of alpha4 phosphoprotein and Sp1 in rat lymphoma cells. J. Cell. Biochem. 2005, 96:579-588.