Mechanisms of mineralocorticoid action: Determinants of receptor specificity and actions of regulated gene products

Trends in Endocrinology and Metabolism

Volumn 15, Issue 4, 2004, Pages 147-153

  Bhargava, Aditi ^a   Pearce, David ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; GLUCOCORTICOID RECEPTOR; ISOPROTEIN; MINERALOCORTICOID; MINERALOCORTICOID RECEPTOR; PROTEIN KINASE; SERINE; SODIUM CHANNEL; UBIQUITIN; UBIQUITIN PROTEIN LIGASE NEDD4;

DNA BINDING; EPITHELIUM; GENE CONTROL; GENE TARGETING; GENETIC CODE; HUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; SODIUM TRANSPORT; TISSUE SPECIFICITY;

ANIMALS; HUMANS; IMMEDIATE-EARLY PROTEINS; MINERALOCORTICOIDS; NUCLEAR PROTEINS; PROTEIN-SERINE-THREONINE KINASES; PROTEINS; RECEPTORS, MINERALOCORTICOID;

EID: 1942518228     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tem.2004.03.009     Document Type: Review

References (81)

1. Grundy H.M., et al. Isolation of a highly active mineralocorticoid from beef adrenal extract. Nature. 169:1952;795-796.
2. Simpson S.A., et al. Isolierung eines neuen kristallisierten hormons aus nebennieren mit besonerer hoher wirksamkeit auf den mineralostoff wechsel. Experientia. 9:1953;333.
3. Funder J.W. Aldosterone action: new answers, new questions. Mol. Cell. Endocrinol. 151:1999;1-3.
4. Young M.J., Funder J.W. Mineralocorticoid receptors and pathophysiological roles for aldosterone in the cardiovascular system. J. Hypertens. 20:2002;1465-1468.
5. Ganong W.F., Mulrow P.J. Rate of change in sodium and potassium excretion after injection of aldosterone into the aorta and renal artery of the dog. Am. J. Physiol. 195:1958;337-342.
6. Crabbe J. Site of action of aldosterone on the toad bladder. Nature. 200:1963;787-788.
7. Edelman I.S., et al. On the mechanism of action of aldosterone on sodium transport: the role of protein synthesis. Proc. Natl. Acad. Sci. U. S. A. 50:1963;1169-1176.
8. Edelman I.S., Fimognari G.M. On the biochemical mechanism of action of aldosterone. Recent Prog. Horm. Res. 24:1968;1-44.
9. Tomkins G.M., Martin D.W. Jr. Hormones and gene expression. Annu. Rev. Genet. 4:1970;91-106.
10. Rousseau G., et al. Glucocorticoid and mineralocorticoid receptors for aldosterone. J. Steroid Biochem. 3:1972;219-227.
11. Funder J.W., et al. Glucocorticoid receptors in rat kidney: the binding of tritiated-dexamethasone. Endocrinology. 92:1973;1005-1013.
12. Chandler V.L., et al. DNA sequences bound specifically by glucocorticoid receptor in vitro render a heterologous promoter hormone responsive in vivo. Cell. 33:1983;489-499.
13. Yamamoto K.R. Steroid receptor regulated transcription of specific genes and gene networks. Annu. Rev. Genet. 19:1985;209-252.
14. Yudt M.R., Cidlowski J.A. The glucocorticoid receptor: coding a diversity of proteins and responses through a single gene. Mol. Endocrinol. 16:2002;1719-1726.
15. Pearce D., et al. Aldosterone: its receptor, target genes, and actions. Vitam. Horm. 66:2003;29-76.
16. Evans R.M. The steroid and thyroid hormone receptor superfamily. Science. 240:1988;889-895.
17. Pearce D., Yamamoto K.R. Mineralocorticoid and glucocorticoid receptor activities distinguished by nonreceptor factors at a composite response element. Science. 259:1993;1161-1165.
18. Rupprecht R., et al. Transactivation and synergistic properties of the mineralocorticoid receptor: relationship to the glucocorticoid receptor. Mol. Endocrinol. 7:1993;597-603.
19. Arriza J.L., et al. Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science. 237:1987;268-275.
20. Diamond M.I., et al. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 249:1990;1266-1272.
21. Tanaka M., Herr W. Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell. 60:1990;375-386.
22. Drouin J., et al. Novel glucocorticoid receptor complex with DNA element of the hormone-repressed POMC gene. EMBO J. 12:1993;145-156.
23. Ray A., Prefontaine K.E. Physical association and functional antagonism between the p65 subunit of transcription factor NF-kappa B and the glucocorticoid receptor. Proc. Natl. Acad. Sci. U. S. A. 91:1994;752-756.
24. Meijer O.C., et al. Transcriptional repression of the 5-HT1A receptor promoter by corticosterone via mineralocorticoid receptors depends on the cellular context. J. Neuroendocrinol. 12:2000;245-254.
25. Courey A.J. Cooperativity in transcriptional control. Curr. Biol. 11:2001;R250-R252.
26. Herschlag D., Johnson F.B. Synergism in transcriptional activation: a kinetic view. Genes Dev. 7:1993;173-179.
27. Liu W., et al. Steroid receptor transcriptional synergy is potentiated by disruption of the DNA-binding domain dimer interface. Mol. Endocrinol. 10:1996;1399-1406.
28. Liu W., et al. Steroid receptor heterodimerization demonstrated in vitro and in vivo. Proc. Natl. Acad. Sci. U. S. A. 92:1995;12480-12484.
29. Iniguez-Lluhi J.A., Pearce D. A common motif within the negative regulatory regions of multiple factors inhibits their transcriptional synergy. Mol. Cell. Biol. 20:2000;6040-6050.
30. Mahajan R., et al. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140:1998;259-270.
31. Yeh E.T., et al. Ubiquitin-like proteins: new wines in new bottles. Gene. 248:2000;1-14.
32. Janne O.A., et al. Androgen-receptor-interacting nuclear proteins. Biochem. Soc. Trans. 28:2000;401-405.
33. Liu B., et al. Inhibition of Stat1-mediated gene activation by PIAS1. Proc. Natl. Acad. Sci. U. S. A. 95:1998;10626-10631.
34. Rogers R.S., et al. SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation. J. Biol. Chem. 278:2003;30091- 30097.
35. Tallec L.P., et al. Protein inhibitor of activated signal transducer and activator of transcription 1 interacts with the N-terminal domain of mineralocorticoid receptor and represses its transcriptional activity: implication of small ubiquitin-related modifier 1 modification. Mol. Endocrinol. 17:2003;2529-2542.
36. Holmstrom S., et al. Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy. Proc. Natl. Acad. Sci. U. S. A. 100:2003;15758-15763.
37. Pearce D., et al. Determinants of subnuclear organization of mineralocorticoid receptor characterized through analysis of wild type and mutant receptors. J. Biol. Chem. 277:2002;1451-1456.
38. Kumar V., Chambon P. The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell. 55:1988;145-156.
39. Wrange O., et al. The purified activated glucocorticoid receptor is a homodimer. J. Biol. Chem. 264:1989;5253-5259.
40. Dahlman-Wright K., et al. Interaction of the glucocorticoid receptor DNA-binding domain with DNA as a dimer is mediated by a short segment of five amino acids. J. Biol. Chem. 266:1991;3107-3112.
41. Adams M., et al. Homodimerization of the glucocorticoid receptor is not essential for response element binding: activation of the phenylethanolamine N-methyltransferase gene by dimerization-defective mutants. Mol. Endocrinol. 17:2003;2583-2592.
42. Kaspar F., et al. A mutant androgen receptor from patients with Reifenstein syndrome: identification of the function of a conserved alanine residue in the D box of steroid receptors. Mol. Cell. Biol. 13:1993;7850-7858.
43. Reichardt H.M., et al. DNA binding of the glucocorticoid receptor is not essential for survival. Cell. 93:1998;531-541.
44. Poukka H., et al. Ubc9 interacts with the androgen receptor and activates receptor- dependent transcription. J. Biol. Chem. 274:1999;19441-19446.
45. Kitagawa H., et al. Ligand-selective potentiation of rat mineralocorticoid receptor activation function 1 by a CBP-containing histone acetyltransferase complex. Mol. Cell. Biol. 22:2002;3698-3706.
46. Webster M.K., et al. Immediate-early transcriptional regulation and rapid mRNA turnover of a putative serine/threonine protein kinase. J. Biol. Chem. 268:1993;11482-11485.
47. Chen S.-Y., et al. Epithelial sodium channel regulated by aldosterone-induced protein sgk. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2514-2519.
48. Naray-Fejes-Toth A., et al. SGK is an aldosterone-induced kinase in the renal collecting duct. Effects on epithelial Na+ channels. J. Biol. Chem. 274:1999;16973-16978.
49. Loffing J., et al. Aldosterone induces rapid apical translocation of ENaC in early portion of renal collecting system: possible role of SGK. Am. J. Physiol. Renal. Physiol. 280:2001;F675-F682.
50. Wang J., et al. SGK integrates insulin and mineralocorticoid regulation of epithelial sodium transport. Am. J. Physiol. Renal. Physiol. 280:2001;F303-F313.
51. Brennan F.E., Fuller P.J. Rapid upregulation of serum and glucocorticoid-regulated kinase (sgk) gene expression by corticosteroids in vivo. Mol. Cell. Endocrinol. 166:2000;129-136.
52. Shigaev A., et al. Regulation of sgk by aldosterone and its effects on the epithelial Na(+) channel. Am. J. Physiol. Renal Physiol. 278:2000;F613-F619.
53. Bhargava A., et al. The serum- and glucocorticoid-induced kinase is a physiological mediator of aldosterone action. Endocrinology. 142:2001;1587-1594.
54. Hollister R.D., et al. Distribution of the messenger RNA for the extracellularly regulated kinases 1, 2 and 3 in rat brain: effects of excitotoxic hippocampal lesions. Neuroscience. 79:1997;1111-1119.
55. Imaizumi K., et al. Differential expression of sgk mRNA, a member of the Ser/Thr protein kinase gene family, in rat brain after CNS injury. Brain Res. Mol. Brain Res. 26:1994;189-196.
56. Waldegger S., et al. Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc. Natl. Acad. Sci. U. S. A. 94:1997;4440-4445.
57. Rozansky D.J., et al. Hypotonic induction of SGK1 and Na+ transport in A6 cells. Am. J. Physiol. Renal Physiol. 283:2002;F105-F113.
58. Alliston T.N., et al. Follicle stimulating hormone-regulated expression of serum/glucocorticoid-inducible kinase in rat ovarian granulosa cells: a functional role for the Sp1 family in promoter activity. Mol. Endocrinol. 11:1997;1934-1949.
59. Naray-Fejes-Toth A., Fejes-Toth G. The sgk, an aldosterone-induced gene in mineralocorticoid target cells, regulates the epithelial sodium channel. Kidney Int. 57:2000;1290-1294.
60. Rozansky D.J., et al. Hypotonic induction of SGK1 and Na(+) transport in A6 cells. Am. J. Physiol. Renal Physiol. 283:2002;F105-F113.
61. Waldegger S., et al. Cloning of sgk serine-threonine protein kinase from shark rectal gland - a gene induced by hypertonicity and secretagogues. Pflugers Arch. 436:1998;575-580.
62. Chen S.Y., et al. Epithelial sodium channel regulated by aldosterone-induced protein sgk. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2514-2519.
63. Naray-Fejes-Toth A., et al. sgk is an aldosterone-induced kinase in the renal collecting duct. Effects on epithelial na+ channels. J. Biol. Chem. 274:1999;16973-16978.
64. Wagner C.A., et al. Effects of the serine/threonine kinase SGK1 on the epithelial Na(+) channel (ENaC) and CFTR: implications for cystic fibrosis. Cell. Physiol. Biochem. 11:2001;209-218.
65. Faletti C.J., et al. sgk: an essential convergence point for peptide and steroid hormone regulation of ENaC-mediated Na(+) transport. Am. J. Physiol. Cell Physiol. 282:2002;C494-C500.
66. Helms M.N., et al. Hormone-regulated transepithelial Na+ transport in mammalian CCD cells requires SGK1 expression. Am. J. Physiol. Renal Physiol. 284:2003;F480-F487.
67. Yun C.C., et al. The serum and glucocorticoid-inducible kinase SGK1 and the Na(+)/H(+) exchange regulating factor NHERF2 synergize to stimulate the renal outer medullary K(+) channel ROMK1. J. Am. Soc. Nephrol. 13:2002;2823-2830.
68. Alvarez de la Rosa D., et al. The serum and glucocorticoid kinase sgk increases the abundance of epithelial sodium channels in the plasma membrane of Xenopus oocytes. J. Biol. Chem. 274:1999;37834-37839.
69. Bhargava, A. et al. Regulation of epithelial ion transportby aldosterone through chnages in gene expression. Mol. Cell. Endocrinol. (in press).
70. Wulff, P. et al. (2001) Deficient salt retention in the SGK1 knockout mouse. In Am. Soc. Neph. Annual Mtg. (Vol. 12) pp. 44A, Appears in JASN.
71. Wang J., et al. SGK integrates insulin and mineralocorticoid regulation of epithelial sodium transport. Am. J. Physiol. Renal Physiol. 280:2001;F303-F313.
72. Debonneville C., et al. Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression. EMBO J. 20:2001;7052-7059.
73. Snyder P.M., et al. Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel. J. Biol. Chem. 277:2002;5-8.
74. Kamynina E., et al. A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel. FASEB J. 15:2001;204-214.
75. Zecevic, M. et al. (2004) SGK1 increases Na,K-ATP cell-surface expression and function in Xenopus laevis oocytes. Pflugers Arch.
76. Chun J., et al. Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 1. J. Biochem. (Tokyo). 133:2003;103-108.
77. Lang F., et al. Regulation of channels by the serum and glucocorticoid-inducible kinase - implications for transport, excitability and cell proliferation. Cell. Physiol. Biochem. 13:2003;41-50.
78. Brunet A., et al. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a). Mol. Cell. Biol. 21:2001;952-965.
79. Kobayashi T., et al. Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem. J. 344:1999;189-197.
80. Kobayashi T., et al. Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase. Biochem. J. 344:1999;189-197.
81. Friedrich B., et al. The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na(+) channel alpha,beta,gamma-ENaC. Pflugers Arch. 445:2003;693-696.