Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRγ

Biochemical and Biophysical Research Communications

Volumn 312, Issue 4, 2003, Pages 975-982

  Hentschke, Moritz ^a   Borgmeyer, Uwe ^a  

^a UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Activation function; ERR3; Groucho; NR3B3; Orphan nuclear receptor; Phage display; PNRC; Transactivation; Transcription factor

Indexed keywords

BACTERIAL PROTEIN; CELL NUCLEUS RECEPTOR; COMPLEMENTARY DNA; ESTROGEN RELATED RECEPTOR GAMMA; HYBRID PROTEIN; POLYPEPTIDE; PROLINE RICH NUCLEAR RECEPTOR COREGULATOR PROTEIN 2; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR TLE1; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; DNA LIBRARY; GENETIC CODE; GENOME ANALYSIS; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; RECEPTOR BINDING; REPORTER GENE;

BACTERIA (MICROORGANISMS);

EID: 0344064200     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.025     Document Type: Article

References (45)

1. Mangelsdorf D.J., Thummel C., Beato M., Herrlich P., Schütz G., Umesono K., Blumberg B., Kastner P., Mark M., Chambon P., Evans R.M. The nuclear receptor superfamily: the second decade. Cell. 83:1995;835-839.
2. Green S., Chambon P. Nuclear receptors enhance our understanding of transcription regulation. Trends Genet. 4:1988;309-314.
3. McKenna N.J., O'Malley B.W. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell. 108:2002;465-474.
4. Hermanson O., Glass C.K., Rosenfeld M.G. Nuclear receptor coregulators: multiple modes of modification. Trends Endocrinol. Metab. 13:2002;55-60.
5. Onate S.A., Tsai S.Y., Tsai M.-J., O'Malley B.W. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 270:1995;1354-1357.
6. Chen J.D., Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 377:1995;454-457.
7. Hörlein A.J., Näär A.M., Heinzel T., Torchia J., Gloss B., Kurokawa R., Ryan A., Kamei Y., Söderström M., Glass C.K., Rosenfeld M.G. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature. 377:1995;397-404.
8. Heinzel T., Lavinsky R.M., Mullen T.M., Soderstrom M., Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature. 387:1997;43-48.
9. Nagy L., Kao H.Y., Chakravarti D., Lin R.J., Hassig C.A., Ayer D.E., Schreiber S.L., Evans R.M. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell. 89:1997;373-380.
10. Giguére V., Yang N., Segui P., Evans R.M. Identification of a new class of steroid hormone receptors. Nature. 331:1988;91-94.
11. Sladek R., Bader J.A., Giguëre V. The orphan nuclear receptor estrogen-related receptor alpha is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene. Mol. Cell. Biol. 17:1997;5400-5409.
12. Pettersson K., Svensson K., Mattsson R., Carlsson B., Ohlsson R., Berkenstam A. Expression of a novel member of estrogen response element-binding nuclear receptors is restricted to the early stages of chorion formation during mouse embryogenesis. Mech. Dev. 54:1996;211-223.
13. Giguére V. To ERR in the estrogen pathway. Trends Endocrinol. Metab. 13:2002;220-225.
14. Süsens U., Hermans-Borgmeyer I., Borgmeyer U. Alternative splicing and expression of the mouse estrogen receptor-related receptor (ERR) γ Biochem. Biophys. Res. Commun. 267:2000;532-535.
15. Lorke D.E., Süsens U., Borgmeyer U., Hermans-Borgmeyer I. Differential expression of the estrogen receptor-related receptor (ERR) γ in the mouse brain. Brain Res. Mol. Brain. Res. 77:2000;277-280.
16. Hermans-Borgmeyer I., Süsens U., Borgmeyer U. Developmental expression of the estrogen receptor-related receptor (ERR) γ during mouse embryogenesis. Mech. Dev. 97:2000;197-199.
17. Hentschke M., Süsens U., Borgmeyer U. Domains of ERRγ that mediate homodimerization and interaction with factors stimulating DNA binding. Eur. J. Biochem. 269:2002;4086-4097.
18. Hentschke M., Süsens U., Borgmeyer U. PGC-1 and PERC, coactivators of the estrogen receptor-related receptor. Biochem. Biophys. Res. Commun. 299:2002;872-879.
19. Hong H., Yang L., Stallcup M.R. Hormone-independent transcriptional activation and coactivator binding by novel orphan nuclear receptor ERR3. J. Biol. Chem. 274:1999;22618-22626.
20. Lu D., Kiriyama Y., Lee K.Y., Giguere V. Transcriptional regulation of the estrogen-inducible pS2 breast cancer marker gene by the ERR family of orphan nuclear receptors. Cancer Res. 61:2001;6755-6761.
21. Greschik H., Wurtz J.M., Sanglier S., Bourguet W., van Dorsselaer A., Moras D., Renaud J.P. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell. 9:2002;303-313.
22. Hentschke M., Schulze C., Süsens U., Borgmeyer U. Characterization of calmodulin binding to the orphan nuclear receptor ERRγ Biol. Chem. 384:2003;473-482.
23. Puigserver P., Wu Z., Park C.W., Graves R., Wright M., Spiegelman B.M. A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell. 92:1998;829-839.
24. Kressler D., Schreiber S.N., Knutti D., Kralli A. The PGC-1-related protein PERC is a selective coactivator of estrogen receptor α J. Biol. Chem. 277:2002;13918-13925.
25. Lin J., Puigserver P., Donovan J., Tarr P., Spiegelman B.M. Peroxisome proliferator-activated receptor γ coactivator 1β (PGC-1β), a novel PGC-1-related transcription coactivator associated with host cell factor. J. Biol. Chem. 277:2002;1645-1648.
26. Huss J.M., Kopp R.P., Kelly D.P. PGC-1. α coactivates the cardiac-enriched nuclear receptors ERR α and γ via novel leucine-rich interaction interfaces J. Biol. Chem. 277:2002;40265-40274.
27. Berry M., Metzger D., Chambon P. Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J. 9:1990;2811-2818.
28. Metzger D., Ali S., Bornert J.M., Chambon P. Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells. J. Biol. Chem. 270:1995;9535-9542.
29. Guan K.L., Dixon J.E. Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:1991;262-267.
30. Umesono K., Murakami K.K., Thompson C.C., Evans R.M. Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptors. Cell. 65:1991;1255-1266.
31. Schmitz T.P., Süsens U., Borgmeyer U. DNA binding, protein interaction and differential expression of the human germ cell nuclear factor. Biochim. Biophys. Acta. 1446:1999;173-180.
32. Zhou D., Chen S. PNRC2 is a 16. kDa coactivator that interacts with nuclear receptors through an SH3-binding motif Nucleic Acids Res. 29:2001;3939-3948.
33. Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., Artavanis-Tsakonas S. Human homologs of a Drosophila Enhancer of split gene product define a novel family of nuclear proteins. Nat. Genet. 2:1992;119-127.
34. Umesono K., Evans R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell. 57:1989;1139-1146.
35. He T.C., Chan T.A., Vogelstein B., Kinzler K.W. PPARδ is an APC-regulated target of nonsteroidal anti-inflammatory drugs. Cell. 99:1999;335-345.
36. Zhou D., Quach K.M., Yang C., Lee S.Y., Pohajdak B., Chen S. PNRC: a proline-rich nuclear receptor coregulatory protein that modulates transcriptional activation of multiple nuclear receptors including orphan receptors SF1 (steroidogenic factor 1) and ERRα1 (estrogen related receptor α-1). Mol. Endocrinol. 14:2000;986-998.
37. Courey A.J., Jia S. Transcriptional repression: the long and the short of it. Genes Dev. 15:2001;2786-2796.
38. Fisher A., Caudy M. The function of hairy-related bHLH repressor proteins in cell fate decisions. Bioessays. 20:1998;298-306.
39. Dehni G., Liu Y., Husain J., Stifani S. TLE expression correlates with mouse embryonic segmentation, neurogenesis, and epithelial determination. Mech. Dev. 53:1995;369-381.
40. Yao J., Liu Y., Husain J., Lo R., Palaparti A., Henderson J., Stifani S. Combinatorial expression patterns of individual TLE proteins during cell determination and differentiation suggest non-redundant functions for mammalian homologs of Drosophila Groucho. Dev. Growth Differ. 40:1998;133-146.
41. Yu X., Li P., Roeder R.G., Wang Z. Inhibition of androgen receptor-mediated transcription by amino-terminal enhancer of split. Mol. Cell. Biol. 21:2001;4614-4625.
42. Flores-Saaib R.D., Jia S., Courey A.J. Activation and repression by the C-terminal domain of dorsal. Development. 128:2001;1869-1879.
43. Conlan R.S., Gounalaki N., Hatzis P., Tzamarias D. The Tup1-Cyc8 protein complex can shift from a transcriptional co-repressor to a transcriptional co-activator. J. Biol. Chem. 274:1999;205-210.
44. Heard D.J., Norby P.L., Holloway J., Vissing H. Human ERRγ, a third member of the estrogen receptor-related receptor (ERR) subfamily of orphan nuclear receptors: tissue-specific isoforms are expressed during development and in the adult. Mol. Endocrinol. 14:2000;382-392.
45. Lepourcelet M., Shivdasani R.A. Characterization of a novel mammalian Groucho isoform and its role in transcriptional regulation. J. Biol. Chem. 277:2002;47732-47740.