Activation and repression of glucose-stimulated ChREBP requires the concerted action of multiple domains within the MondoA conserved region

American Journal of Physiology - Endocrinology and Metabolism

Volumn 299, Issue 4, 2010, Pages

  Davies, Michael N ^a   O'Callaghan, Brennon L ^a   Towle, Howard C ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Carbohydrate response element binding protein; Glucose signaling; Lipogenesis; Transcription

Indexed keywords

BINDING PROTEIN; CARBOHYDRATE RESPONSE ELEMENT BINDING PROTEIN; GLUCOSE; PROTEIN MONDOA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; RENILLA LUCIFERIN 2 MONOOXYGENASE; WBSCR14 PROTEIN, RAT;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; GLYCOLYSIS; HUMAN; HUMAN CELL; MAMMAL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; WILD TYPE; ANIMAL; ANTAGONISTS AND INHIBITORS; BINDING COMPETITION; CELL LINE; CHEMISTRY; DNA RESPONSIVE ELEMENT; GEL MOBILITY SHIFT ASSAY; GENE EXPRESSION REGULATION; GENETIC TRANSFECTION; GENETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PLASMID; PROTEIN TERTIARY STRUCTURE; RAT; SITE DIRECTED MUTAGENESIS;

ANIMALS; BASIC HELIX-LOOP-HELIX LEUCINE ZIPPER TRANSCRIPTION FACTORS; BINDING, COMPETITIVE; CELL LINE; CONSERVED SEQUENCE; ELECTROPHORETIC MOBILITY SHIFT ASSAY; GLUCOSE; LUCIFERASES, RENILLA; MUTAGENESIS, INSERTIONAL; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; RATS; RESPONSE ELEMENTS; TRANSFECTION;

EID: 77957553171     PISSN: 01931849     EISSN: 15221555     Source Type: Journal    
DOI: 10.1152/ajpendo.00349.2010     Document Type: Article

References (26)

1. Billin AN, Eilers AL, Coulter KL, Logan JS, Ayer DE. MondoA, a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. Mol Cell Biol 20: 8845-8854, 2000.
2. Billin AN, Eilers AL, Queva C, Ayer DE. Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. J Biol Chem 274: 36344-36350, 1999.
3. Collier JJ, Zhang P, Pedersen KB, Burke SJ, Haycock JW, Scott DK. c-Myc and ChREBP regulate glucose-mediated expression of the L-type pyruvate kinase gene in INS-1-derived 832/13 cells. Am J Physiol Endocrinol Metab 293: E48-E56, 2007.
4. da Silva Xavier G, Rutter GA, Diraison F, Andreolas C, Leclerc I. ChREBP binding to fatty acid synthase and L-type pyruvate kinase genes is stimulated by glucose in pancreatic beta-cells. J Lipid Res 47: 2482-2491, 2006.
5. Davies MN, O'Callaghan BL, Towle HC. Glucose activates ChREBP by increasing its rate of nuclear entry and relieving repression of its transcriptional activity. J Biol Chem 283: 24029-24038, 2008.
6. Eckert DT, Zhang P, Collier JJ, O'Doherty RM, Scott DK. Detailed molecular analysis of the induction of the L-PK gene by glucose. Biochem Biophys Res Commun 372: 131-136, 2008.
7. Eilers AL, Sundwell E, Lin M, Sullivan AA, Ayer DE. A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex. Mol Cell Biol 22: 8514-8526, 2002.
8. Hillgartner FB, Salati LM, Goodridge AG. Physiological and molecular mechanisms involved in nutritional regulation of fatty acid synthesis. Physiol Rev 75: 47-76, 1995.
9. Hohmeier HE, Mulder H, Chen G, Henkel-Rieger R, Prentki M, Newgard CB. Isolation of INS-1-derived cell lines with robust ATP-sensitive K+ channel-dependent and -independent glucose-stimulated insulin secretion. Diabetes 49: 424-430, 2000.
10. Iizuka K, Bruick RK, Liang G, Horton JD, Uyeda K. Deficiency of carbohydrate response element-binding protein (ChREBP) reduces lipogenesis as well as glycolysis. Proc Natl Acad Sci USA 101: 7281-7286, 2004.
11. Kabashima T, Kawaguchi T, Wadzinski BE, Uyeda K. Xylulose 5-phosphate mediates glucose-induced lipogenesis by xylulose 5-phosphate-activated protein phosphatase in rat liver. Proc Natl Acad Sci USA 100: 5107-5112, 2003.
12. Kawaguchi T, Takenoshita M, Li Y, 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 98: 13710-13715, 2001.
13. Li MV, Chang B, Imamura M, Poungvarin N, Chan L. Glucose-dependent transcriptional regulation by an evolutionarily conserved glucose-sensing module. Diabetes 55: 1179-1189, 2006.
14. Li MV, Chen W, Poungvarin N, Imamura M, Chan L. Glucose-mediated transactivation of carbohydrate response element-binding protein requires cooperative actions from Mondo conserved regions and essential trans-acting factor 14-3-3. Mol Endocrinol 22: 1658-1672, 2008.
15. Ma L, Tsatsos NG, Towle HC. Direct role of ChREBP.Mlx in regulating hepatic glucose-responsive genes. J Biol Chem 280: 12019-12027, 2005.
16. Merla G, Howald C, Antonarakis SE, Reymond A. The subcellular localization of the ChoRE-binding protein, encoded by the Williams-Beuren syndrome critical region gene 14, is regulated by 14-3-3. Hum Mol Genet 13: 1505-1514, 2004.
17. 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 19: 3266-3277, 2000.
18. Peterson CW, Stoltzman CA, Sighinolfi MP, Han KS, Ayer DE. Glucose controls nuclear accumulation, promoter binding, and transcriptional activity of the MondoA-Mlx heterodimer. Mol Cell Biol 30: 2887-2895, 2010.
19. Sakiyama H, Wynn RM, Lee WR, Fukasawa M, Mizuguchi H, Gardner KH, Repa JJ, 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 283: 24899-24908, 2008.
20. Sans CL, Satterwhite DJ, Stoltzman CA, Breen KT, Ayer DE. MondoA-Mlx heterodimers are candidate sensors of cellular energy status: mitochondrial localization and direct regulation of glycolysis. Mol Cell Biol 26: 4863-4871, 2006.
21. 14 gene. Context of the CACGTG motif determines the specificity of carbohydrate regulation. J Biol Chem 269: 9380-9387, 1994.
22. Stoeckman AK, Ma L, Towle HC. Mlx is the functional heteromeric partner of the carbohydrate response element-binding protein in glucose regulation of lipogenic enzyme genes. J Biol Chem 279: 15662-15669, 2004.
23. Tsatsos NG, Davies MN, O'Callaghan BL, Towle HC. Identification and function of phosphorylation in the glucose-regulated transcription factor ChREBP. Biochem J 411: 261-270, 2008.
24. Tsatsos NG, Towle HC. Glucose activation of ChREBP in hepatocytes occurs via a two-step mechanism. Biochem Biophys Res Commun 340: 449-456, 2006.
25. Yamashita H, Takenoshita M, Sakurai M, Bruick RK, Henzel WJ, Shillinglaw W, Arnot D, Uyeda K. A glucose-responsive transcription factor that regulates carbohydrate metabolism in the liver. Proc Natl Acad Sci USA 98: 9116-9121, 2001.
26. Zhang P, Metukuri MR, Bindom SM, Prochownik EV, O'Doherty RM, Scott DK. c-Myc is required for the CHREBP-dependent activation of glucose-responsive genes. Mol Endocrinol 24: 1274-1286, 2010.