T cell leukemia-associated human Notch/translocation-associated Notch homologue has IκB-like activity and physically interacts with nuclear factor-κB proteins in T cells

Journal of Experimental Medicine

Volumn 183, Issue 5, 1996, Pages 2025-2032

  Guan, Ennan ^a,c   Wang, Jinhai ^a   Laborda, Jorge ^a   Norcross, Michael ^a   Baeuerle, Patrick A ^b   Hoffman, Thomas ^a  

^a CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^b AMGEN INC   (United States)

^c Federal Drug Administration   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MEMBRANE RECEPTOR;

ARTICLE; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN PROTEIN INTERACTION; T CELL LEUKEMIA; TRANSCRIPTION REGULATION;

ANIMALS; CELL LINE; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 7; CHROMOSOMES, HUMAN, PAIR 9; HUMANS; INVERTEBRATES; LEUKEMIA, T-CELL; MEMBRANE PROTEINS; NF-KAPPA B; PROTO-ONCOGENE PROTEINS; RECEPTOR, NOTCH1; RECEPTORS, CELL SURFACE; RECEPTORS, NOTCH; RECOMBINANT FUSION PROTEINS; T-LYMPHOCYTES; TRANS-ACTIVATION (GENETICS); TRANSCRIPTION FACTOR RELB; TRANSCRIPTION FACTORS; TRANSLOCATION, GENETIC; TUMOR CELLS, CULTURED; VERTEBRATES;

EID: 0029980867     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.183.5.2025     Document Type: Article

References (54)

1. Kidd, S., M.K. Baylies, G.P. Gasic, and M.W. Young. 1989. Structure and distribution of the Notch protein in developing Drosophila [published erratum appears in Genes & Dev. 1989 Dec;3(12A):2020]. Genes & Dev. 3:1113-1129.
2. Heitzler, P., and P. Simpson. 1993. Altered epidermal growth factor-like sequences provide evidence for a role of Notch as a receptor in cell fate decisions. Development (Camb.). 117: 1113-1123.
3. Yochem, J., and I. Greenwald. 1989. glp-1 and lin-12, genes implicated in distinct cell-cell interactions in C. elegans, encode similar transmembrane proteins. Cell. 58:553-563.
4. Yochem, J., K. Weston, and I. Greenwald. 1988. The Caenorhabditis elegans lin-12 gene encodes a transmembrane protein with overall similarity to Drosophila Notch. Nature (Lond.). 335:547-550.
5. Greenwald, I., and G. Seydoux. 1990. Analysis of gain-of-function mutations of the lin-12 gene of Caenorhabditis elegant. Nature (Lond.). 346:197-199.
6. Artavanis-Tsakonas, S., and P. Simpson. 1991. Choosing a cell fate: a view from the Notch locus. Trends Genet. 7:403-408.
7. Greenwald, I., and G.M. Rubin. 1992. Making a difference: the role of cell-cell interactions in establishing separate identities for equivalent cells. Cell. 68:271-281.
8. Ellisen, L.W., J. Bird, D.C. West, A.L. Soreng, T.C. Reynolds, S.D. Smith, and J. Sklar. 1991. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell. 66: 649-661.
9. Zagouras, P., S. Stifani, C.M. Blaumueller, M.L. Carcangiu, and S. Artavanis-Tsakonas. 1995. Alterations in Notch signaling in neoplastic lesions of the human cervix. Proc. Natl. Acad. Sci. USA. 92:6414-6418.
10. Lindsell, C.E., C.J. Shawber, J. Boulter, and G. Weinmaster. 1995. Jagged: a mammalian ligand that activates Notch1. Cell. 80:909-917.
11. Fehon, R.G., P.J. Kooh, I. Rebay, C.L. Regan, T. Xu, M.A. Muskavitch, and S. Artavanis-Tsakonas. 1990. Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell. 61:523-534.
12. Roehl, H., and J. Kimble. 1993. Control of cell fate in C. elegans by a GLP-1 peptide consisting primarily of ankyrin repeats. Nature (Lond.). 364:632-635.
13. Kopan, R., J.S. Nye, and H. Weintraub. 1994. The intracellular domain of mouse Notch: a constitutively activated repressor of myogenesis directed at the basic helix-loop-helix region of MyoD. Development (Camb.). 120:2385-2396.
14. Artavanis-Tsakonas, S., K. Matsuno, and M.E. Fortini. 1995. Notch signaling. Science (Wash. DC). 268:225-232.
15. Baeuerle, P.A., and T. Henkel. 1994. Function and activation of NF-kappa B in the immune system. Annu. Rev. Immunol. 12:141-179.
16. Baeuerle, P.A. 1991. The inducible transcription activator NF-kappa B: regulation by distinct protein subunits. Biochim. Biophys. Acta. 1072:63-80.
17. Kawakami, K., C. Scheidereit, and R.G. Roeder. 1988. Identification and purification of a human immunoglobulin-enhancer-binding protein (NF-kappa B) that activates transcription from a human immunodeficiency virus type 1 promoter in vitro. Proc. Natl. Acad. Sci. USA. 85:4700-4704.
18. Baeuerle, P.A., and D. Baltimore. 1988. I kappa B: a specific inhibitor of the NF-kappa B transcription factor. Science (Wash. DC). 242:540-546.
19. Bours, V., J. Villalobos, P.R. Burd, K. Kelly, and U. Siebenlist. 1990. Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding protein with homology to the rel oncogene and to cell-cycle motifs. Nature (Lond.). 348:76-80.
20. Ruben, S.M., J.F. Klement, T.A. Coleman, M. Maher, C.H. Chen, and C.A. Rosen. 1992. I-Rel: a novel rel-related protein that inhibits NF-kappa B transcriptional activity. Genes & Dev. 6:745-760.
21. Gilmore, T.D. 1990. NF-kappa B, KBF1, dorsal, and related matters. Cell. 62:841-843.
22. Schmid, R.M., N.D. Perkins, C.S. Duckett, P.C. Andrews, and G.J. Nabel. 1991. Cloning of an NF-kappa B subunit which stimulates HIV transcription in synergy with p65. Nature (Lond.). 352:733-736.
23. Kieran, M., V. Blank, F. Logeat, J. Vandekerckhove, F. Lottspeich, O. Le Bail, M.B. Urban, P. Kourilsky, P.A. Baeuerle, and A. Israel. 1990. The DNA binding subunit of NF-kappa B is identical to factor KBF1 and homologous to the rel oncogene product. Cell. 62:1007-1018.
24. Ghosh, S., and D. Baltimore. 1990. Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature (Lond.). 344:678-682.
25. Nolan, G.P., S. Ghosh, H.C. Liou, P. Tempst, and D. Baltimore. 1991. DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide. Cell. 64:961-969.
26. Duckett, C.S., N.D. Perkins, T.F. Kowalik, R.M. Schmid, E.S. Huang, A.S. Baldwin, Jr., and G.J. Nabel. 1993. Dimerization of NF-KB2 with RelA(p65) regulates DNA binding, transcriptional activation, and inhibition by an I kappa B-alpha (MAD-3). Mol. Cell. Biol. 13:1315-1322.
27. Beg, A.A., and A.S. Baldwin, Jr. 1993. The I kappa B proteins: multifunctional regulators of Rel/NF-kappa B transcription factors. Genes & Dev. 7:2064-2070.
28. Schmitz, M.L., and P.A. Baeuerle. 1991. The p65 subunit is responsible for the strong transcription activating potential of NF-kappa B. EMBO (Eur. Mol. Biol. Organ.) J. 10:3805-3817.
29. Haskill, S., A.A. Beg, S.M. Tompkins, J.S. Morris, A.D. Yurochko, A. Sampson-Johannes, K. Mondal, P. Ralph, and A.S. Baldwin, Jr. 1991. Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity. Cell 65:1281-1289.
30. Wulczyn, F.G., M. Naumann, and C. Scheidereit. 1992. Candidate proto-oncogene bcl-3 encodes a subunit-specific inhibitor of transcription factor NF-kappa B. Nature (Lond.). 358:597-599.
31. Franzoso, G., V. Bours, S. Park, M. Tomita-Yamaguchi, K. Kelly, and U. Siebenlist. 1992. The candidate oncoprotein Bcl-3 is an antagonist of p50/NF-kappa B-mediated inhibition. Nature (Lond.). 359:339-342.
32. Inoue, J., L.D. Kerr, D. Rashid, N. Davis, H.R. Bose, Jr., and I.M. Verma. 1992. Direct association of pp40/I kappa B beta with rel/NF-kappa B transcription factors: role of ankyrin repeats in the inhibition of DNA binding activity. Proc. Natl. Acad. Sci. USA. 89:4333-4337.
33. Franzoso, G., P. Biswas, G. Poli, L.M. Carlson, K.D. Brown, M. Tomita-Yamaguchi, A.S. Fauci, and U.K. Siebenlist. 1994. A family of serine proteases expressed exclusively in myelo-monocytic cells specifically processes the nuclear factor-κB subunit p65 in vitro and may impair human immunodeficiency virus replication in these cells. J. Exp. Med. 180: 1445-1456.
34. Hatada, E.N., A. Nieters, F.G. Wulczyn, M. Naumann, R. Meyer, G. Nucifora, T.W. McKeithan, and C. Scheidereit. 1992. The ankyrin repeat domains of the NF-kappa B precursor p105 and the protooncogene bcl-3 act as specific inhibitors of NF-kappa B DNA binding. Proc. Natl. Acad. Sci. USA. 89:2489-2493.
35. Davis, N., S. Ghosh, D.L. Simmons, P. Tempst, H.C. Liou, D. Baltimore, and H.R. Bose, Jr. 1991. Rel-associated pp40: an inhibitor of the rel family of transcription factors. Science (Wash. DC). 253:1268-1271.
36. Shirakawa, F., and S.B. Mizel. 1989. In vitro activation and nuclear translocation of NF-kappa B catalyzed by cyclic AMP-dependent protein kinase and protein kinase C. Mol. Cell Biol. 9:2424-2430.
37. Kerr, L.D., C.S. Duckett, P. Wamsley, Q. Zhang, P. Chiao, G. Nabel, T.W. McKeithan, P.A. Baeuerle, and I.M. Verma. 1992. The proto-oncogene bcl-3 encodes an I kappa B protein. Genes & Dev. 6:2352-2363.
38. Henkel, T., T. Machleidt, I. Alkalay, M. Kronke, Y. Ben-Neriah, and P.A. Baeuerle. 1993. Rapid proteolysis of I kappa B-alpha is necessary for activation of transcription factor NF-kappa B. Nature (Lond.). 365:182-185.
39. Naumann, M., F.G. Wulczyn, and C. Scheidereit. 1993. The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3 are I kappa B molecules and control nuclear translocation of NF- kappa B. EMSO (Eur. Mol. Biol. Organ.) J. 12: 213-222.
40. Bours, V., G. Franzoso, V. Azarenko, S. Park, T. Kanno, K. Brown, and U. Siebenlist. 1993. The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers. Cell. 72:729-739.
41. Ohno, H., G. Takimoto, and T.W. McKeithan. 1990. The candidate proto-oncogene bcl-3 is related to genes implicated in cell lineage determination and cell cycle control. Cell. 60: 991-997.
42. Dignam, J.D., R.M. Lebovitz, and R.G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475-1489.
43. + T lymphocytes. Science (Wash. DC). 256:1452-1456.
44. Matsuno, K., R.J. Diederich, M.J. Go, C.M. Blaumueller, and S. Artavanis-Tsakonas. 1995. Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats. Development (Camb.). 121:2633-2644.
45. Tannahill, D., S. Bray, and W.A. Harris. 1995. A Drosophila E(spl) gene is neurogenic in Xenopus: a green fluorescent protein study. Dev. Biol. 168:694-697.
46. Jennings, B., A. Preiss, C. Delidakis, and S. Bray. 1994. The Notch signalling pathway is required for Enhancer of split bHLH protein expression during neurogenesis in the Drosophila embryo. Development (Camb.). 120:3537-3548.
47. Fortini, M.E., I. Rebay, L.A. Caron, and S. Artavanis-Tsakonas. 1993. An activated Notch receptor blocks cell-fate commitment in the developing Drosophila eye. Nature (Lond.). 365:555-557.
48. Jarriault, S., C. Brou, F. Logeat, E.H. Schroeter, R. Kopan, and A. Israel. 1995. Signalling downstream of activated mammalian Notch. Nature (Lond.). 377:355-358.
49. Lux, S.E., K.M. John, and V. Bennett. 1990. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature (Lond.). 344:36-42.
50. Thompson, C.C., T.A. Brown, and S.L. McKnight. 1991. Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex [see comments]. Science (Wash. DC). 253:762-768.
51. Rebay, I., R.G. Fehon, and S. Artavanis-Tsakonas. 1993. Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor. Cell. 74: 319-329.
52. Robbins, J., B.J. Blondel, D. Gallahan, and R. Callahan. 1992. Mouse mammary tumor gene int-3: a member of the notch gene family transforms mammary epithelial cells. J. Virol. 66:2594-2599.
53. Moore, B.E., and H.R. Bose, Jr. 1988. Expression of the v-rel oncogene in reticuloendotheliosis virus-transformed fibroblasts. Virology. 162:377-387.
54. Sylla, B.S., and H.M. Temin. 1986. Activation of oncogenicity of the c-rel proto-oncogene. Mol. Cell Biol. 6:4709-4716.