Defining an N-terminal activation domain of the orphan nuclear receptor Nurr1

Biochemical and Biophysical Research Communications

Volumn 313, Issue 1, 2004, Pages 205-211

  Nordzell, Mariette ^a   Aarnisalo, Piia ^a,c   Benoit, Gérard ^a   Castro, Diogo S ^a,d   Perlmann, Thomas ^a,b  

^a LUDWIG INSTITUTE FOR CANCER RESEARCH   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF HELSINKI   (Finland)

^d NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

Activation function; Nuclear receptor; Orphan receptor; Phosphorylation; Transcription

Indexed keywords

LIGAND; MITOGEN ACTIVATED PROTEIN KINASE; NUCLEAR RECEPTOR RELATED FACTOR 1; TRANSCRIPTION FACTOR AP 1;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL SPECIFICITY; CELL TYPE; CONTROLLED STUDY; DOPAMINERGIC NERVE CELL; EMBRYO; ENZYME ACTIVATION; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MESENCEPHALON; MUTAGENESIS; NERVE GROWTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

EID: 0346220219     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.079     Document Type: Article

References (36)

1. Truss M., Beato M. Steroid hormone receptors: interaction with deoxyribonucleic acid and transcription factors. Endocrinol. Rev. 14:1993;459-479.
2. Mangelsdorf D.J., Thummel C., Beato M., Herrlich P., Schutz G., Umesono K., Blumberg B., Kastner P., Mark M., Chambon P.et al. The nuclear receptor superfamily: the second decade. Cell. 83:1995;835-839.
3. Le W.D., Xu P., Jankovic J., Jiang H., Appel S.H., Smith R.G., Vassilatis D.K. Mutations in NR4A2 associated with familial Parkinson disease. Nat. Genet. 33:2003;85-89.
4. Milbrandt J. Nerve growth factor induces a gene homologous to the glucocorticoid receptor gene. Neuron. 1:1988;183-188.
5. Law S.W., Conneely O.M., DeMayo F.J., O'Malley B.W. Identification of a new brain-specific transcription factor, NURR1. Mol. Endocrinol. 6:1992;2129-2135.
6. Maruyama K., Tsukada T., Ohkura N., Bandoh S., Hosono T., Yamaguchi K. The NGFI-B subfamily of the nuclear receptor superfamily (review). Int. J. Oncol. 12:1998;1237-1243.
7. Perlmann T., Jansson L. A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1. Genes Dev. 9:1995;769-782.
8. Forman B.M., Umesono K., Chen J., Evans R.M. Unique response pathways are established by allosteric interactions among nuclear hormone receptors. Cell. 81:1995;541-550.
9. Mangelsdorf D.J., Evans R.M. The RXR heterodimers and orphan receptors. Cell. 83:1995;841-850.
10. Germain P., Iyer J., Zechel C., Gronemeyer H. Co-regulator recruitment and the mechanism of retinoic acid receptor synergy. Nature. 415:2002;187-192.
11. Philips A., Lesage S., Gingras R., Maira M.H., Gauthier Y., Hugo P., Drouin J. Novel dimeric Nur77 signaling mechanism in endocrine and lymphoid cells. Mol. Cell. Biol. 17:1997;5946-5951.
12. Castro D.S., Arvidsson M., Bondesson Bolin M., Perlmann T. Activity of the Nurr1 carboxyl-terminal domain depends on cell type and integrity of the activation function 2. J. Biol. Chem. 274:1999;37483-37490.
13. Glass C.K., Rosenfeld M.G. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 14:2000;121-141.
14. Wang Z., Benoit G., Liu J., Prasad S., Aarnisalo P., Liu X., Xu H., Walker N.P., Perlmann T. Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors. Nature. 423:2003;555-560.
15. Weigel N.L. Steroid hormone receptors and their regulation by phosphorylation. Biochem. J. 319:1996;657-667.
16. Ali S., Metzger D., Bornert J.M., Chambon P. Modulation of transcriptional activation by ligand-dependent phosphorylation of the human oestrogen receptor A/B region. EMBO J. 12:1993;1153-1160.
17. Kato S., Endoh H., Masuhiro Y., Kitamoto T., Uchiyama S., Sasaki H., Masushige S., Gotoh Y., Nishida E., Kawashima H.et al. Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science. 270:1995;1491-1494.
18. Bunone G., Briand P.A., Miksicek R.J., Picard D. Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J. 15:1996;2174-2183.
19. Hu E., Kim J.B., Sarraf P., Spiegelman B.M. Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma. Science. 274:1996;2100-2103.
20. Adams M., Reginato M.J., Shao D., Lazar M.A., Chatterjee V.K. Transcriptional activation by peroxisome proliferator-activated receptor gamma is inhibited by phosphorylation at a consensus mitogen-activated protein kinase site. J. Biol. Chem. 272:1997;5128-5132.
21. Camp H.S., Tafuri S.R. Regulation of peroxisome proliferator-activated receptor gamma activity by mitogen-activated protein kinase. J. Biol. Chem. 272:1997;10811-10816.
22. Taneja R., Rochette-Egly C., Plassat J.L., Penna L., Gaub M.P., Chambon P. Phosphorylation of activation functions AF-1 and AF-2 of RAR alpha and RAR gamma is indispensable for differentiation of F9 cells upon retinoic acid and cAMP treatment. EMBO J. 16:1997;6452-6465.
23. Hammer G.D., Krylova I., Zhang Y., Darimont B.D., Simpson K., Weigel N.L., Ingraham H.A. Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: integration of hormone signaling in reproduction and stress. Mol. Cell. 3:1999;521-526.
24. Davis I.J., Hazel T.G., Chen R.H., Blenis J., Lau L.F. Functional domains and phosphorylation of the orphan receptor Nur77. Mol. Endocrinol. 7:1993;953-964.
25. Zhang Y., Beck C.A., Poletti A., Clement J.P.T., Prendergast P., Yip T.T., Hutchens T.W., Edwards D.P., Weigel N.L. Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo. Mol. Endocrinol. 11:1997;823-832.
26. Joel P.B., Smith J., Sturgill T.W., Fisher T.L., Blenis J., Lannigan D.A. pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. Mol. Cell. Biol. 18:1998;1978-1984.
27. Fahrner T.J., Carroll S.L., Milbrandt J. The NGFI-B protein, an inducible member of the thyroid/steroid receptor family, is rapidly modified posttranslationally. Mol. Cell. Biol. 10:1990;6454-6459.
28. Hazel T.G., Misra R., Davis I.J., Greenberg M.E., Lau L.F. Nur77 is differentially modified in PC12 cells upon membrane depolarization and growth factor treatment. Mol. Cell. Biol. 11:1991;3239-3246.
29. Hirata Y., Kiuchi K., Chen H.C., Milbrandt J., Guroff G. The phosphorylation and DNA binding of the DNA-binding domain of the orphan nuclear receptor NGFI-B. J. Biol. Chem. 268:1993;24808-24812.
30. Katagiri Y., Hirata Y., Milbrandt J., Guroff G. Differential regulation of the transcriptional activity of the orphan nuclear receptor NGFI-B by membrane depolarization and nerve growth factor. J. Biol. Chem. 272:1997;31278-31284.
31. Li Y., Lau L.F. Adrenocorticotropic hormone regulates the activities of the orphan nuclear receptor Nur77 through modulation of phosphorylation. Endocrinology. 138:1997;4138-4146.
32. Wallen A.A., Castro D.S., Zetterstrom R.H., Karlen M., Olson L., Ericson J., Perlmann T. Orphan nuclear receptor nurr1 is essential for ret expression in midbrain dopamine neurons and in the brain stem. Mol. Cell. Neurosci. 18:2001;649-663.
33. Benoit G.R., Flexor M., Besancon F., Altucci L., Rossin A., Hillion J., Balajthy Z., Legres L., Segal-Bendirdjian E., Gronemeyer H., Lanotte M. Autonomous rexinoid death signaling is suppressed by converging signaling pathways in immature leukemia cells. Mol. Endocrinol. 15:2001;1154-1169.
34. Paulsen R.E., Weaver C.A., Fahrner T.J., Milbrandt J. Domains regulating transcriptional activity of the inducible orphan receptor NGFI-B. J. Biol. Chem. 267:1992;16491-16496.
35. Katagiri Y., Takeda K., Yu Z.-X., Ferrans V.J., Ozato K., Garoff G. Modulation of retinoid signalling through NGF-induced nuclear export. Nat. Cell Biol. 2:2000;435-440.
36. Wansa K.D., Harris J.M., Muscat G.E. The activation function-1 domain of Nur77/NR4A1 mediates trans-activation, cell specificity, and coactivator recruitment. J. Biol. Chem. 277:2002;33001-33011.