Distinct functional properties of IκBα and IκBβ

Molecular and Cellular Biology

Volumn 17, Issue 9, 1997, Pages 5386-5399

  Tran, Kathy ^a   Merika, Menie ^a   Thanos, Dimitris ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; DNA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN;

ANIMAL CELL; ARTICLE; COMPLEX FORMATION; DNA BINDING; DNA PROTEIN COMPLEX; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; TRANSCRIPTION REGULATION;

ANIMALIA; ESCHERICHIA COLI;

EID: 0030745885     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.9.5386     Document Type: Article

References (67)

1. Arenzana-Seisdedos, F., J. Thompson, M. S. Rodriguez, F. Bacherlerie, D. Thomas, and R. T. Hay. 1995. Inducible nuclear expression of newly synthesized IκBα negatively regulates DNA-binding and transcriptional activities of NF-κB. Mol. Cell. Biol. 15:2689-2696.
2. Baeuerle, P. A., and D. Baltimore. 1988. IκB: a specific inhibitor of the NF-κB transcription factor. Science 242:540-546.
3. Baeuerle, P. A., and D. Baltimore. 1996. NF-κB: ten years after. Cell 87:13-20.
4. Baeuerle, P. A., and T. Henkel. 1994. Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 12:141-179.
5. Baldi, L., K. Brown, G. Franzoso, and U. Siebenlist. 1996. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IκBα. J. Biol. Chem. 271:376-379.
6. Baldwin, A. S., Jr. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649-681.
7. Barroga, C. F., J. K. Stevenson, E. M. Schwarz, and I. M. Verma. 1995. Constitutive phosphorylation of IκBα by casein kinase II. Proc. Natl. Acad. Sci. USA 92:7637-7641.
8. Beauparlant, P., R. Lin, and J. Hiscott. 1996. The role of C-terminal domain of IκBα in protein degradation and stabilization. J. Biol. Chem. 271:10690-10696.
9. Beg, A. A., and A. S. Baldwin, Jr. 1993. The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev. 7:2064-2070.
10. Beg, A. A., S. M. Ruben, R. I. Scheinman, S. Haskill, C. A. Rosen, and A. S. Baldwin, Jr. 1992. IκB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1899-1913.
11. Beg, A. A., T. S. Finco, P. V. Nantermet, and A. S. Baldwin, Jr. 1993. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: a mechanism for NF-κB activation. Mol. Cell. Biol. 13:3301-3310.
12. Beg, A. A., W. C. Sha, R. T. Bronson, and D. Baltimore. 1996. Constitutive NF-κB activation, enhanced granulopoiesis, and neonatal lethality in IκBα-deficient mice. Genes Dev. 9:2736-2746.
13. Bours, V., G. Franzoso, V. Azarenko, S. Park, T. Kanno, K. Brown, and U. Siebenlist. 1993. The oncoprotein Bcl-3 directly transactivates through κB motifs via association with DNA binding p50B homodimers. Cell 72:729-739.
14. Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκBα proteolysis by site-specific, signal-induced phosphorylation. Science 267:1485-1488.
15. Brown, K., S. Park, T. Kanno, G. Franzoso, and U. Siebenlist. 1993. Mutual regulation of the transcriptional activator NF-κB and its inhibitor. IκBα. Proc. Natl. Acad. Sci. USA 90:2532-2536.
16. Chen, Z. J., L. Parent, and T. Maniatis. 1996. Site-specific phosphorylation of IκBα by a novel ubiquitination-dependent protein kinase activity. Cell 84:853-862.
17. Chiao, P. J., S. Miyamoto, and I. Verma. 1994. Autoregulation of IκBα activity Proc. Natl. Acad. Sci. USA 91:22-25.
18. Chu, Z.-L., T. A. McKinsey, L. Liu, X. Qi, and D. W. Ballard. 1996. Basal phosphorylation of the PEST domain in IκBβ regulates its functional interaction with the c-rel proto-oncogene product. Mol. Cell. Biol. 16:5974-5984.
19. de Martin, R., B. Vanhove, Q. Cheng, E. Hofer, V. Csizmadia, H. Winkler, and F. Bach. 1993. Cytokine inducible expression in endothelial cells of an IκBα gene is regulated by NF-κB. EMBO J. 12:2773-2779.
20. Ernst, M. K., L. L. Dunn, and N. Rice. 1995. The PEST-like sequence in IκBα is responsible for inhibition of DNA binding but not cytoplasmic retention of c-Rel or RelA homodimers. Mol. Cell. Biol. 15:872-882.
21. Finco, T. S., and A. S. Baldwin, Jr. 1995. Mechanistic aspects of NF-κB regulation: the emerging role of phosphorylation and proteolysis. Immunity 3:263-272.
22. Fujita, T., G. P. Nolan, H. C. Liu, M. L. Scott, and D. Baltimore. 1993. The candidate proto-oncogene Bcl-3 encodes a transcriptional co-activator that activates through NF-κB p50 homodimers. Genes Dev. 7:1354-1363.
23. Ghosh, G., G. Van Duyne, S. Ghosh, and P. B. Sigler. 1995. Structure of NF-κB p50 homodimer bound to a κB site. Nature 373:303-310.
24. Good, L., and S. Sun. 1996. Persistent activation of NF-κB/Rel by human T-cell leukemia virus type 1 Tax involves degradation of IκBβ. J. Virol. 70:2730-2735.
25. Grilli, M., J. J-S. Chiu, and M. Lenardo. 1993. NF-κB and Rel: participants in a multiform transcriptional regulatory system. Int. Rev. Cytol. 143:1-62.
26. Haskill, S., A. A. Beg, S. M. Tompkins, J. S. Morris, A. D. Yurochko, A. Sampson-Johanne, K. Mondal, P. Ralph, and A. S. Baldwin. 1991. Characterization of an immediate early gene induced in adherent monocytes that encodes IκB-like activity. Cell 65:1281-1289.
27. Hawley, D. K., and R. G. Roeder. 1985. Separation and partial characterization of three functional steps in transcription initiation by human RNA polymerase II. J. Biol. Chem. 260:8163-8172.
28. Hawley, D. K. 1987. Functional steps in transcription initiation and reinitiation from the major late promoter in a HeLa nuclear extract. J. Biol. Chem. 262:3452-3461.
29. Henkel, T., T. Machleid, I. Alkalay, M. Kronke, Y. Benneriah, and P. A. Baeuerle. 1993. Rapid proteolysis of IκBα is necessary for activation of transcription factor NF-κB. Nature 365:182-185.
30. Ito, C. Y., A. G. Kazantsef, and A. S. Baldwin, Jr. 1994. Three NF-κB sites in the IκBα promoter are required for induction of gene expression by TNF-α. Nucleic Acids Res. 22:3787-3792.
31. Kerr, L. D., J.-I. Inoue, N. Davis, E. Link, P. A. Baeuerle, H. R. Bose, Jr., and I. M. Verma. 1991. The Rel-associated pp40 protein prevents DNA binding of rel and NF-αB - relationship with IκBβ and regulation by phosphorylation. Genes Dev. 5:1464-1476.
32. Klement, J. F., N. R. Rice, B. D. Car, S. J. Abbondanzo, G. D. Powers, P. H. Bhatt, C. H. Chen, C. A. Rosen, and C. L. Stewart. 1996. IκBα deficiency results in a sustained NF-κB response and severe widespread dermatitis in mice. Mol. Cell. Biol. 16:2341-2349.
33. Kretzchmar, M., M. Meisternest, C. Scheidereit, G. Li, and R. G. Roeder. 1992. Transcriptional regulation of the HIV-1 promoter by NF-κB in vitro. Genes Dev. 6:761-774.
34. Kuenzel, E. A., J. A. Mulligan, J. Sommercorn, and E. G. Krebs. 1987. Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides. J. Biol. Chem. 262:9136-9140.
35. LeBail, O., R. Schmidt-Ullrich, and A. Israel. 1993. Promoter analysis of the gene encoding the IκBα/MAD-3 inhibitor of NF-κB: positive regulation by members of the Rel/NF-κB family. EMBO J. 12:5043-5049.
36. Lehming, N., S. McGuire, J. M. Brickman, and M. Ptashne. 1995. Interactions of a Rel protein with its inhibitor. Proc. Natl. Acad. Sci. USA 92:10242-10246.
37. Lin, R., D. Gewert, and J. Hiscott. 1995. Differential transcriptional activation in vitro by NF-κB/Rel proteins. J. Biol. Chem. 270:3123-3131.
38. Lin, R., P. Beauparlant, C. Makris, S. Meloche, and J. Hiscott. 1996. Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability. Mol. Cell. Biol. 16:1401-1409.
39. Lin, Y., K. Brown, and U. Siebenlist. 1995. Activation of NF-κB requires proteolysis of the inhibitor IκB-α: signal-induced phosphorylation of IκB-α alone does not release active NF-κB. Proc. Natl. Acad. Sci. USA 92:552-556.
40. Lin, Y. S., and M. Green. 1991. Mechanism of action of an acidic transcriptional activator in vitro. Cell 64:971-981.
41. Link, E., L. D. Kerr, R. Schreck, U. Zabel, I. Verma, and P. A. Baeuerle. 1992. Purified IκBβ is inactivated upon dephosphorylation. J. Biol. Chem. 267:239-246.
42. MacGregor, G. R., and C. T. Caskey. 1989. Construction of plasmids that express E. coli beta galactosidase in mammalian cells. Nucleic Acids Res. 17:2365.
43. McKinsey, T. A., J. A. Brockman, D. C. Scherer, S. W. Al-Murrani, P. L. Green, and D. W. Ballard. 1996. Inactivation of IκBβ by the Tax protein of human T-cell leukemia virus type 1: a potential mechanism for constitutive induction of NF-κB. Mol. Cell. Biol. 16:2083-2090.
44. Morin, P. J., G. S. Subramanian, and T. D. Gilmore. 1993. GAL4-I kappa B alpha and GAL4-I kappa B gamma activate transcription by different mechanisms. Nucleic Acids Res. 21:2157-2163.
45. Muller, C. W., F. A. Rey, M. Sodeoka, G. L. Verdine, and S. C. Harrison. 1995. Structure of the NF-κB p50 homodimer bound to DNA. Nature 373: 311-317.
46. Palvimo, J., and A. Linnala-Kankkunen. 1989. Identification of sites on chromosomal protein HMG I phosphorylated by casein kinase II. FEBS Lett. 257:101-104.
47. Read, M. A., A. S. Neish, M. E. Gerritsen, and T. Collins. 1996. Post-induction transcriptional repression of E-selectin and VCAM-1. J. Immunol. 157:3472-3479.
48. Roeder, R. G. 1996. The role of general initiation factors in transcription by RNA polymerase II. Trends Biochem. Sci. 21:327-335.
49. Sachdev, S., E. M. Rottjakob, J. A. Diehl, and M. Hannink. 1995. IκBα-mediated inhibition of nuclear transport and DNA binding by Rel proteins are separable functions: phosphorylation of C-terminal serine residues of IκBα is specifically required for inhibition of DNA binding. Oncogene 11:811-823.
50. Sadowski, I., B. Bell, P. Broad, and M. Hollis. 1992. GAL4 fusion vectors for expression in yeast or mammalian cells. Gene 18:137-141.
51. Scherer, D. C., J. A. Brockman, Z. Chen, T. Maniatis, and D. W. Ballard. 1995. Signal-induced degradation of IκBα requires site-specific ubiquitination. Proc. Natl. Acad. Sci. USA 92:11259-11263.
52. Schwarz, W. M., D. V. Antwerp, and I. M. Verma. 1996. Constitutive phosphorylation of IκBα by casein kinase II occurs preferentially at serine 293: requirement for degradation of free IκBα. Mol. Cell. Biol. 16:3554-3559.
53. Scott, M. L., T. Fujita, H. C. Liu, G. P. Nolan, and D. Baltimore. 1993. The p65 subunit of NF-κB regulates IκB by two distinct mechanisms. Genes Dev. 7:1266-1276.
54. Siebenlist, U., G. Franzoso, and K. Brown. 1994. Structure, regulation and function of NF-κB. Annu. Rev. Cell Biol. 10:405-455.
55. Silver, P. A., L. P. Keegan, and M. Ptashne. 1984. Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc. Natl. Acad. Sci. USA 81:5951-5955.
56. Sun, S. C., P. A. Ganchi, D. W. Ballard, and W. C. Greene. 1993. NF-κB controls expression of inhibitor IκBα. Evidence for an inducible autoregulatory pathway. Science 259:1912-1915.
57. Suyang, H., R. Phillips, I. Douglas, and S. Ghosh. 1996. Role of unphosphorylated, newly synthesized IκBβ in persistent activation of NF-κB. Mol. Cell. Biol. 16:5444-5449.
58. Thanos, D., and T. Maniatis. 1992. The high mobility group protein HMG I(Y) is required for NF-κB-dependent virus induction of the human IFN-β gene. Cell 71:777-789.
59. Thanos, D., and T. Maniatis. 1995. Identification of the rel family members required for virus induction of the human beta interferon gene. Mol. Cell. Biol. 15:152-164.
60. Thanos, D., and T. Maniatis. 1995. NF-κB: a lesson in family values. Cell 80:529-532.
61. Thompson, J. E., R. J. Phillips, H. Erdjument-Bromage, P. Tempst, and S. Ghosh. 1995. IκBβ regulates the persistent response in a biphasic activation of NF-κB. Cell 80:573-582.
62. Traenckner, E. B., H. Pahl, T. Henkel, K. N. Schmidt, S. Wilk, and P. A. Baeuerle. 1995. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:2876-2883.
63. Van Antwerp, D. J., and I. M. Verma. 1996. Signal-induced degradation of IκBα: association with NF-κB and the PEST sequence in IκBα are not required. Mol. Cell. Biol. 16:6037-6045.
64. Verma, I., J. K. Stevenson, E. M. Schwarz, D. V. Antwerp, and S. Miyamoto. 1995. Rel/NF-κB/IκB family: intimate tales of association and dissociation. Genes Dev. 9:2723-2735.
65. Yie, J., M. Merika, G. Chen, and D. Thanos. Unpublished data.
66. Zabel, U., and P. A. Baeuerle. Purified human IκB can rapidly dissociate the complex of the NF-κB transcription factor with its cognate DNA. Cell 61: 255-265.
67. Zabel, U., T. Henkel, M. S. Silva, and P. A. Baeuerle. 1993. Nuclear uptake control of NF-κB by MAD-3, an IκB protein present in the nucleus. EMBO J. 12:201-211.