Characterization of calmodulin binding to the orphan nuclear receptor ERRγ

Biological Chemistry

Volumn 384, Issue 3, 2003, Pages 473-482

  Hentschke, Moritz ^a   Schulze, Christian ^a   Süsens, Ute ^a   Borgmeyer, Uwe ^a  

^a UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Calcium; Protein interaction; Second messenger; Transciptional regulation; Transcription factor

Indexed keywords

CALMODULIN; CELL NUCLEUS RECEPTOR; ESTROGEN RECEPTOR; LUCIFERASE; SEPHAROSE;

ANIMAL CELL; BINDING SITE; BIOSENSOR; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DNA BINDING; IN VITRO STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN INTERACTION; RECEPTOR BINDING; REPORTER GENE; REVIEW; SURFACE PLASMON RESONANCE; TRANSCRIPTION INITIATION;

ANIMALS; BINDING SITES; CALCIUM SIGNALING; CALMODULIN; CELL LINE; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; PROTEIN INTERACTION MAPPING; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECEPTORS, ESTROGEN; RECOMBINANT FUSION PROTEINS; SURFACE PLASMON RESONANCE; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTORS;

ANIMALIA;

EID: 0037625758     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.053     Document Type: Review

References (56)

1. Bading, H. (2000). Transcription-dependent neuronal plasticity the nuclear calcium hypothesis. Eur. J. Biochem. 267, 5280-5283.
2. Biswas, D. K., Reddy, P. V., Pickard, M., Makkad, B., Pettit, N., and Pardee, A. B. (1998). Calmodulin is essential for estrogen receptor interaction with its motif and activation of responsive promoter. J. Biol. Chem. 273, 33817-33824.
3. Bouhoute, A., and Leclercq, G. (1996). Calmodulin decreases the estrogen binding capacity of the estrogen receptor. Biochem. Biophys. Res. Commun. 227, 651-657.
4. Bouhoute, A., and Yamashita, K. (1995). Modulation of estradiol and DNA binding to estrogen receptor upon association with calmodulin. Biochem. Biophys. Res. Commun. 208, 748-755.
5. 2+-calmodulin. Mol. Endocrinol. 2, 167-174.
6. Chawla, S., Hardingham, G. E., Quinn, D. R., and Bading, H. (1998). CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science 281, 1505-1509.
7. Clarke, R., Leonessa, F., Welch, J. N., and Skaar, T. C. (2001). Cellular and molecular pharmacology of antiestrogen action and resistance. Pharmacol. Rev. 53, 25-72.
8. Coward, P., Lee, D., Hull, M. V., and Lehmann, J. M. (2001). 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor γ. Proc. Natl. Acad. Sci. USA 98, 8880-8884.
9. Crivici, A., and Ikura, M. (1995). Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24, 85-116.
10. Deisseroth, K., Heist, E. K., and Tsien, R. W. (1998). Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons. Nature 392, 198-202.
11. Garcia Pedrero, J. M., Del Rio, B., Martinez-Campa, C., Muramatsu, M., Lazo, P. S., and Ramos, S. (2002). Calmodulin is a selective modulator of estrogen receptors. Mol. Endocrinol. 16, 947-960.
12. Giguère, V. (2002). To ERR in the estrogen pathway. Trends Endocrinol. Metab. 13, 220-225.
13. Green, S., and Chambon, P. (1988). Nuclear receptors enhance our understanding of transcription regulation. Trends Genet. 4, 309-314.
14. Greschik, H., Wurtz, J. M., Sanglier, S., Bourguet, W., van Dorsselaer, A., Moras, D., and Renaud, J. P. (2002). Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell 9, 303-313.
15. Hardingham, G. E., Chawla, S., Johnson, C. M., and Bading, H. (1997). Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression. Nature 385, 260-265.
16. 2+ channel blocker, barnidipine, reduces platelet-derived growth factor B-chain mRNA in glomeruli of spontaneously hypertensive rats. Am. J. Nephrol. 19, 615-621.
17. He, T. C., Chan, T. A., Vogelstein, B., and Kinzler, K. W. (1999). PPARδ is an APC-regulated target of nonsteroidal anti-inflammatory drugs. Cell 99, 335-345.
18. Heinzer, C., Süsens, U., Schmitz, T. P., and Borgmeyer, U. (1998). Retinoids induce differential expression and DNA binding of the mouse germ cell nuclear factor in P19 embryonal carcinoma cells. Biol. Chem. 379, 349-359.
19. Hentschke, M., Süsens, U., and Borgmeyer, U. (2002a). Domains of ERRγ that mediate homodimerization and interaction with factors stimulating DNA binding. Eur. J. Biochem. 269, 4086-4097.
20. Hentschke, M., Süsens, U., and Borgmeyer, U. (2002b). PGC-1 and PERC, coactivators of the estrogen receptor-related receptor. Biochem. Biophys. Res. Commun. 299, 872-879.
21. Hermans-Borgmeyer, I., Süsens, U., and Borgmeyer, U. (2000). Developmental expression of the estrogen receptor-related receptor (ERR) γ during mouse embryogenesis. Mech. Dev. 97, 197-199.
22. Hoeflich, K. P., and Ikura, M. (2002). Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108, 739-742.
23. Hong, H., Yang, L., and Stallcup, M. R. (1999). Hormone-independent transcriptional activation and coactivator binding by novel orphan nuclear receptor ERR3. J. Biol. Chem. 274, 22618-22626.
24. Ikura, M., Osawa, M., and Ames, J. B. (2002). The role of calcium-binding proteins in the control of transcription: structure to function. Bioessays 24, 625-636.
25. Jurado, L. A., Chockalingam, P. S., and Jarrett, H. W. (1999). Apocalmodulin. Physiol. Rev. 79, 661-682.
26. Karlsson, R., and Falt, A. (1997). Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 200, 121-133.
27. Karlsson, R., Michaelsson, A., and Mattsson, L. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 145, 229-240.
28. Kraus, R. J., Ariazi, E. A., Farrell, M. L., and Mertz, J. E. (2002). Estrogen-related receptor α1 actively antagonizes estrogen receptor-regulated transcription in MCF-7 mammary cells. J. Biol. Chem. 277, 24826-24834.
29. 2+/calmodulin-dependent kinase kinase peptide. J. Mol. Biol. 312, 59-68.
30. Lam, H. Y. (1984). Tamoxifen is a calmodulin antagonist in the activation of cAMP phosphodiesterase. Biochem. Biophys. Res. Commun. 118, 27-32.
31. Laudet, V. (1997). Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor. J. Mol. Endocrinol. 19, 207-226.
32. Li, Z., Joyal, J. L., and Sacks, D. B. (2001). Calmodulin enhances the stability of the estrogen receptor. J. Biol. Chem. 276, 17354-17360.
33. 2+-dependent binding of tamoxifen to calmodulin isolated from bovine brain. Cancer Res. 50, 2753-2758.
34. Lorke, D. E., Süsens, U., Borgmeyer, U., and Hermans-Borgmeyer, I. (2000). Differential expression of the estrogen receptor-related receptor (ERR) γ in the mouse brain. Brain Res. Mol. Brain. Res. 77, 277-280.
35. Lu, D., Kiriyama, Y., Lee, K. Y., and Giguere, V. (2001). Transcriptional regulation of the estrogen-inducible pS2 breast cancer marker gene by the ERR family of orphan nuclear receptors. Cancer Res. 61, 6755-6761.
36. Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., and Evans, R. M. (1995). The nuclear receptor superfamily: the second decade. Cell 83, 835-839.
37. Mehta, D. V., Kim, Y. S., Dixon, D., and Jetten, A. M. (2002). Characterization of the expression of the retinoid-related, testis-associated receptor (RTR) in trophoblasts. Placenta 23, 281-287.
38. Mermelstein, P. G., Deisseroth, K., Dasgupta, N., Isaksen, A. L., and Tsien, R. W. (2001). Calmodulin priming: nuclear translocation of a calmodulin complex and the memory of prior neuronal activity. Proc. Natl. Acad. Sci. USA 98, 15342-15347.
39. Milikan, J. M., and Bolsover, S. R. (2000). Use of fluorescently labelled calmodulins as tools to measure subcellular calmodulin activation in living dorsal root ganglion cells. Pflüger's Arch. 439, 394-400.
40. O'Brian, C. A., Ioannides, C. G., Ward, N. E., and Liskamp, R. M. (1990). Inhibition of protein kinase C and calmodulin by the geometric isomers cis- and trans-tamoxifen. Biopolymers 29, 97-104.
41. Palfi, A., Kortvely, E., Fekete, E., Kovacs, B., Varszegi, S., and Gulya, K. (2002). Differential calmodulin gene expression in the rodent brain. Life Sci. 70, 2829-2855.
42. Rhoads, A. R., and Friedberg, F. (1997). Sequence motifs for calmodulin recognition. FASEB J. 11, 331-340.
43. Rich, R. L., Hoth, L. R., Geoghegan, K. F., Brown, T. A., LeMotte, P. K., Simons, S. P., Hensley, P., and Myszka, D. G. (2002). Kinetic analysis of estrogen receptor/ligand interactions. Proc. Natl. Acad. Sci. USA 99, 8562-8567.
44. Rowlands, M. G., Budworth, J., Jarman, M., Hardcastle, I. R., McCague, R., and Gescher, A. (1995). Comparison between inhibition of protein kinase C and antagonism of calmodulin by tamoxifen analogues. Biochem. Pharmacol. 50, 723-726.
45. Rupp, R. A. W., Snider, L., and Weintraub, H. (1994). Xenopus embryos regulate the nuclear localization of XMyoD. Genes Dev. 8, 1311-1323.
46. Schulze, C. (2000). Analysing biomolecular interactions: the surface plasmon resonance technique. In: Recent Research Developments in Comparative Biochemistry and Physiology, S. G. Pandalai, ed. (Trivandrum, India: Transworld Research Network), pp. 77-90.
47. Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., and Greene, G. L. (1998). The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95, 927-937.
48. Süsens, U., Aguiluz, J. B., Evans, R. M., and Borgmeyer, U. (1997). The germ cell nuclear factor mGCNF is expressed in the developing nervous system. Dev. Neurosci. 19, 410-420.
49. Süsens, U., Hermans-Borgmeyer, I., and Borgmeyer, U. (2000). Alternative splicing and expression of the mouse estrogen receptor-related receptor (ERR) γ. Biochem. Biophys. Res. Commun. 267, 532-535.
50. Tremblay, G., Bergeron, D., and Giguère, V. (2001). 4-Hydroxytamoxifen is an isoform-specific inhibitor of orphan estrogen-receptor-related (ERR) nuclear receptors β and γ. Endocrinol. 142, 4572-4575.
51. Umesono, K., and Evans, R. M. (1989). Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 57, 1139-1146.
52. Vanacker, J.-M., Pettersson, K., Gustafsson, J.-Å., and Laudet, V. (1999). Transcriptional targets shared by estrogen receptor-related receptors (ERRs) and estrogen receptor (ER) α, but not by ERβ. EMBO J. 18, 4270-4279.
53. Vendrell, M., Pujol, M. J., Tusell, J. M., and Serratosa, J. (1992). Effect of different convulsants on calmodulin levels and proto-oncogene c-fos expression in the central nervous system. Brain Res. Mol. Brain Res. 14, 285-292.
54. Wärnmark, A., Almlöf, T., Leers, J., Gustafsson, J. Å., and Treuter, E. (2001). Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERα and ERβ. J. Biol. Chem. 276, 23397-23404.
55. Wärnmark, A., Treuter, E., Gustafsson, J. Å., Hubbard, R. E., Brzozowski, A. M., and Pike, A. C. (2002). Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor α. J. Biol. Chem. 277, 21862-21868.
56. Yus-Nàjera, E., Santana-Castro, I., and Villarroel, A. (2002). The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels. J. Biol. Chem. 277, 28545-28553.