Role of the repressor JDP2 in the amino acid-regulated transcription of CHOP

FEBS Letters

Volumn 582, Issue 10, 2008, Pages 1537-1541

  Chérasse, Yoan ^a   Chaveroux, Cédric ^a   Jousse, Céline ^a   Maurin, Anne Catherine ^a   Carraro, Valérie ^a   Parry, Laurent ^a   Fafournoux, Pierre ^a   Bruhat, Alain ^a  

^a INRA and University of Auvergne   (France)

Author keywords

Amino acid response element; ATF2; CHOP; JDP2

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 2; ACTIVATING TRANSCRIPTION FACTOR 4; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; HETERODIMER; HISTONE DEACETYLASE 3; HOMODIMER; JUN DIMERIZATION PROTEIN 2; LEUCINE; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN MALNUTRITION; TRANSCRIPTION INITIATION;

DIMERIZATION; GENE EXPRESSION REGULATION; GENES, REPORTER; HELA CELLS; HISTONE DEACETYLASES; HUMANS; LEUCINE; LUCIFERASES; REPRESSOR PROTEINS; TRANSCRIPTION FACTOR CHOP; TRANSCRIPTION, GENETIC;

EID: 42049093407     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.03.050     Document Type: Article

References (17)

1. Young V.R., El-Khoury A.E., Melchor S., and Castillo L. The Biochemistry and Physiology of Protein and Amino Acid Metabolism, With Reference to Protein Nutrition. In: Niels C.R.R. (Ed). Protein Metabolism During Infancy Vol. 33 (1994), Nestec Ltd., Vevey/ Raven Press Ltd., New York 1-28
2. Kilberg M.S., Pan Y.X., Chen H., and Leung-Pineda V. Nutritional control of gene expression: how mammalian cells respond to amino acid limitation. Annu. Rev. Nutr. 25 (2005) 59-85
3. Ron D., and Habener J.F. CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. Genes Dev. 6 (1992) 439-453
4. Bruhat A., Jousse C., Carraro V., Reimold A.M., Ferrara M., and Fafournoux P. Amino acids control mammalian gene transcription: activating transcription factor 2 is essential for the amino acid responsiveness of the CHOP promoter. Mol. Cell Biol. 20 (2000) 7192-7204
5. Bruhat A., Averous J., Carraro V., Zhong C., Reimold A.M., Kilberg M.S., and Fafournoux P. Differences in the molecular mechanisms involved in the transcriptional activation of the CHOP and asparagine synthetase genes in response to amino acid deprivation or activation of the unfolded protein response. J. Biol. Chem. 277 (2002) 48107-48114
6. Bruhat A., Cherasse Y., Maurin A.C., Breitwieser W., Parry L., Deval C., Jones N., Jousse C., and Fafournoux P. ATF2 is required for amino acid-regulated transcription by orchestrating specific histone acetylation. Nucleic Acids Res. 35 (2007) 1312-1321
7. Averous J., Bruhat A., Jousse C., Carraro V., Thiel G., and Fafournoux P. Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation. J. Biol. Chem. 279 (2004) 5288-5297
8. Cherasse Y., Maurin A.C., Chaveroux C., Jousse C., Carraro V., Parry L., Deval C., Chambon C., Fafournoux P., and Bruhat A. The p300/CBP-associated factor (PCAF) is a cofactor of ATF4 for amino acid-regulated transcription of CHOP. Nucleic Acids Res. 35 (2007) 5954-5965
9. Jin C., Ugai H., Song J., Murata T., Nili F., Sun K., Horikoshi M., and Yokoyama K.K. Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2. FEBS Lett. 489 (2001) 34-41
10. Aronheim A., Zandi E., Hennemann H., Elledge S.J., and Karin M. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol. Cell Biol. 17 (1997) 3094-3102
11. Jin C., Li H., Murata T., Sun K., Horikoshi M., Chiu R., and Yokoyama K.K. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Mol. Cell Biol. 22 (2002) 4815-4826
12. Lerdrup M., Holmberg C., Dietrich N., Shaulian E., Herdegen T., Jaattela M., and Kallunki T. Depletion of the AP-1 repressor JDP2 induces cell death similar to apoptosis. Biochim. Biophys. Acta 1745 (2005) 29-37
13. Nakade K., Pan J., Yoshiki A., Ugai H., Kimura M., Liu B., Li H., Obata Y., Iwama M., Itohara S., Murata T., and Yokoyama K.K. JDP2 suppresses adipocyte differentiation by regulating histone acetylation. Cell Death Differ. 14 (2007) 1398-1405
14. Heinrich R., Livne E., Ben-Izhak O., and Aronheim A. The c-Jun dimerization protein 2 inhibits cell transformation and acts as a tumor suppressor gene. J. Biol. Chem. 279 (2004) 5708-5715
15. Breitwieser W., Lyons S., Flenniken A.M., Ashton G., Bruder G., Willington M., Lacaud G., Kouskoff V., and Jones N. Feedback regulation of p38 activity via ATF2 is essential for survival of embryonic liver cells. Genes Dev. 21 (2007) 2069-2082
16. Steinmuller L., and Thiel G. Regulation of gene transcription by a constitutively active mutant of activating transcription factor 2 (ATF2). Biol. Chem. 384 (2003) 667-672
17. Jin C., Kato K., Chimura T., Yamasaki T., Nakade K., Murata T., Li H., Pan J., Zhao M., Sun K., Chiu R., Ito T., Nagata K., Horikoshi M., and Yokoyama K.K. Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2. Nat. Struct. Mol. Biol. 13 (2006) 331-338