Transcription of the dominant-negative helix-loop-helix protein Id1 is regulated by a protein complex containing the immediate-early response gene Egr-1

Molecular and Cellular Biology

Volumn 16, Issue 5, 1996, Pages 2418-2430

  Tournay, Olivia ^a   Benezra, Robert ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CELL DIFFERENTIATION; COMPLEX FORMATION; DNA PROTEIN COMPLEX; DNA SEQUENCE; EARLY RESPONSE GENE; ENHANCER REGION; GENETIC REGULATION; GENETIC TRANSCRIPTION; IMMEDIATE EARLY GENE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SITE DIRECTED MUTAGENESIS; TRANSCRIPTION REGULATION;

ANIMALIA;

EID: 0029914835     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.5.2418     Document Type: Article

References (77)

1. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Siedman, J. A. Smith, and K. Struhl (ed.). 1987. Current protocols in molecular biology John Wiley & Sons, New York.
2. Benezra, R. Unpublished data.
3. Benezra, R., R. L. Davis, D. Lockshon, L. Turner, and H. Weintraub. 1990. The protein Id a negative regulator of helix-loop-helix DNA binding proteins. Cell 61:49-59.
4. Benezra, R., and W. Yan. Unpublished data
5. Biggs, J., E. Murphy, and M. Israel. 1992. A human Id-like helix-loop-helix protein expressed during early development. Proc Natl. Acad Sci. USA 89:1512-1516.
6. Brennan, T. J., and E. N. Olson. 1990. Myogenin resides in the nucleus and acquires high affinity for a conserved enhancer element on heterodimerization. Genes Dev. 4:582-595.
7. Brindle, P. K., and M. R. Montminy. 1992. The CREB family of transcription activators. Curr Opin Genet. Dev. 2:199-204.
8. Cabrera, C. V., and M. C. Alonso. 1991. Transcriptional activation by heterodimers of the achaete-scute and daughterless gene products of Drosophila. EMBO J 10:2965-2973
9. Cao, X., R. Mahendran, G. R. Guy, and Y. H. Tan. 1992. Protein phosphatase inhibitors induce the sustained expression of the Egr-1 gene and the hyperphosphorylation of its gene product. J. Biol. Chem 267:12991-12997.
10. Cao, X., R. Mahendran, G. R. Guy, and Y. H. Tan. 1993. Detection and characterization of cellular Egr-1 binding to its recognition site. J. Biol. Chem. 268:16949-16957.
11. Caudy, M., H. Vassin, M. Brand, R. Tuma, L. Y. Jan, and N. Jan. 1988. daughterless, a Drosophila gene essential for both neurogenesis and sex determination, has sequence similarities to myc and the achuete-scute complex. Cell 55:1061-1067.
12. Christy, B., and D. Nathans. 1989. DNA binding site of the growth factor-inducible proteins Zif268. Proc. Natl. Acad. Sci USA 86:8737-8748.
13. Christy, B. A., L. K. Sanders, L. F. Lau, N. G. Copeland, N. A. Jenlins, and D. Nathans. 1991 An Id-related helix-loop-helix protein encoded by a growth factor-inducible gene Proc. Natl. Acad. Sci. USA 88:1815-1819.
14. Cordle, S. R., E. Henderson, H. Masuoka, P. A. Weil, and R. Stein. 1991 Pancreatic B-cell-type-specific transcription of the insulin gene is mediated by basic helix-loop-helix DNA-binding proteins. Mol Cell Biol. 11:1734-1738
15. Crescenzi, M., T. P. Fleming, A. B. Lassar, H. Weintraub, and S. A. Aaronson. 1990 MyoD induces growth arrest independent of differentiation in normal and transformed cells. Proc. Natl. Acad. Sci USA 87:8442-8446
16. Curran, T., and B. R. Franza, Jr. 1988. Fos and Jun: the AP-1 connection. Cell 55:395-397.
17. Davis, R. L., P. F. Cheng, A. B. Lassar, and H. Weintraub. 1990 The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell 60:773-776.
18. Davis, R. L., H. Weintraub, and A. B. Lassar. 1987. Expression of a single transfected cDNA converts fibroblasts to myoblasts. Cell 51:987-1000
19. Desprez, P.-Y., E. Hara, M. J. Bissell, and J. Campisi. 1995. Suppression of mammary epithelial cell differentiation by the helix-loop-helix protein Id1. Mol. Cell. Biol. 15:3398-3404.
20. Duncan, M., E. M. DiCicco-Bloom, X. Xiang, K. Benezra, and K. Chada. 1992. The gene for the helix-loop-helix proteins, Id, is specifically expressed in neural precursors. Dev. Biol. 154:1-10.
21. Edwards, S. A., T. Darland, R. Sosnowski, M. Samuels, and E. D. Adamson. 1991. The transcription factor Egr-1 is rapidly modulated in response to retinoic acid in P19 embryonal carcinoma cells. Dev Biol. 148:165-173.
22. Ellenberger, T., D. Fass, M. Arnaud, and S. C. Harrison. 1994. Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev 8:970-980
23. Ellmeier, W., A. Aguzzi, E. Kleiner, R. Kurzbauer, and A. Weith. 1992 A mutually exclusive expression of a helix-loop-helix gene and N-myc in human neuroblastomas and in normal development. EMBO J. 11:2563-2571.
24. Ellmeier, W., and A. Weith. 1995. Expression of the helix-loop-helix gene Id3 during murine embryonic development. Dev. Dyn. 203:163-173.
25. Ephrussi, A., G. M. Church, S. Tonegawa, and W. Gilbert. 1985. B lineage-specific interactions of an immunoglobulin enhancer with cellular factors in vivo. Science 227:134-140.
26. Evans, S. M., and T. X. O'Brien. 1993. Expression of the helix-loop-helix factor Id during mouse embryonic development Dev. Biol. 159:485-499.
27. Hara, E., T. Yamaguchi, H. Nojima, T. Ide, J. Campisi, H. Okayama, and K. Oda. 1994. Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts. J. Biol. Chem. 269:2139-2145
28. Henthorn, P., M. Kiledjian, and T. Kadesch. 1990. Two distinct transcription factors that bind the immunoglobulin enhancer μE5/kE2 motif. Science 247:467-470.
29. Higuchi, R. 1990. Recombinant PCR, p. 177-183. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T J. White (ed.), PCR protocols: a guide to methods and applications. Academic Press, Inc , San Diego, Calif.
30. Jan, Y. N., and L. Y. Jan. 1993. HLH proteins, fly neurogenesis, and vertebrate myogenesis. Cell 75:827-830.
31. Jen, Y. Personal communication.
32. Jen, Y., H. Weintraub, and R. Benezra. 1992. Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins. Genes Dev. 6:1466-1479.
33. 3 in rat osteoblastic osteosarcoma cells. Proc. Natl. Acad Sci. USA 89:4569-4572.
34. Kiledjian, M., L. K. Su, and T. Kadesch. 1988. Identification and characterization of two functional domains within the murine heavy-chain enhancer. Mol. Cell. Biol. 8:145-152.
35. Kim, S. J., K. Y. Kim, S. J. Tapscott, T. S. Winokur, K. Park, H. Fujiki, H. Weintraub, and A. B. Roberts. 1992. Inhibition of protein phosphatases blocks myogenesis by first altering MyoD binding activity. J. Biol. Chem. 267:15140-15145.
36. Klambt, C., E. Knust, K. Tietze, and J. A. Campos-Ortega. 1989. Closely related transcripts encoded by the neurogenic gene complex enhancer of split of Drosophila melanogaster. EMBO J. 8:203-210.
37. Kreider, B., R. Benezra, G. Rovera, and T. Kadesch. 1992. Inhibition of myeloid differentiation by the helix-loop-helix Id Science 255:1700-1702.
38. Kurabayashi, M., S. Dutta, and L. Kedes. 1994 Serum inducible factors binding to an activating transcription factor motif regulate transcription of the Id2A promoter during myogenic differentiation. J. Biol. Chem. 269: 31162-31170.
39. Lassar, A. B., J. N. Buskin, D. Lockshon, R. L. Davis, S. Apone, S. D. Hauschka, and H. Weintraub. 1989. MyoD is a sequence-specific DNA protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer Cell 58:823-831.
40. Lassar, A. B., R. L. Davis, W. E. Wright, T. Kadesch, C. Murre, A. Voronova, D. Baltimore, and H. Weintraub. 1991. Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. Cell 66:305-315.
41. Lau, L. F., and D. Nathans. 1987. Expression of a set of growth-related immediate early genes in BALB/c3T3 cells: coordinate relation with c-fos or c-myc. Proc. Natl. Acad. Sci. USA 84:1182-1186.
42. Lemaire, P., O. Revelant, R. Bravo, and P. Charnay. 1988. Two mouse genes encoding potential transcription factors with identical DNA-binding domains are activated by growth factors in cultured cells. Proc. Natl. Acad. Sci. USA 85:4691-4695.
43. Lister, J., W. C. Forrester, and M. H. Baron. 1995. Inhibition of an erythroid differentiation switch by the helix-loop-helix protein Id1. J. Biol Chem. 270:17939-17946.
44. Littlewood, T. D., and G. I. Evan. 1994. Transcription factors 2: helix-loop-helix. Protein Profile 1:639-709.
45. Ma, P. C., M. A. Rould, H. Weintraub, and C. O. Pabo. 1994. Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation. Cell 77:451-459.
46. McMahon, A. P., J. E. Champion, J. A. McMahon, and V. P. Sukhatme. 1990. Developmental expression of the putative transcription factor Egr-1 suggests that Egr-1 and c-fos are co-regulated in some tissues. Development (Cambridge) 108:281-287.
47. Murray, S. S., C. A. Glackin, K. A. Winters, D. Gazit, A. J. Kahn, and E. J. Murray. 1992. Expression of helix-loop-helix regulatory genes during differentiation of mouse osteoblastic cells. J. Bone Miner. Res. 7:1131-1138.
48. Murre, C., P. S. McCaw, and D. Baltimore. 1989. A new DNA binding and dimerazation motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56:777-783
49. Murre, C., P. S. McCaw, H. Vaessin, M. Caudy, L. Y. Jan, Y. N. Jan, C. V. Cabrera, J. N. Buskin, S. D. Hauschka, A. B. Lassar, et al. 1989. Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537-544.
50. Neuhold, L. A., and B. Wold. 1993. HLH forced dimers: tethering MyoD to E47 generates a dominant positive myogenic factor insulated from negative reguration by Id. Cell 74:1033-1042.
51. Noda, M., R. L. Vogel, A. M. Craig, J. Prahl, H. F. DeLuca, and D. T. Denhardt. 1990. Identification of a DNA sequence responsible for binding of the 1,25-dihydroxyvitamin D3 receptor and 1,25-dihydroxyvitamin D3 enhancement of mouse secreted phosphoprotem 1 (SPP-1 or osteopontin) gene expression. Proc. Natl. Acad. Sci USA 87:9995-9999.
52. Olson, E. N., and W. H. Klein. 1994. bHLH factors in muscle development: dead lines and commitments. Genes Dev. 8:1-8.
53. Park, K., M. Chung, and S. J. Kim. 1992. Inhibition of myogenesis by okadaic acid, an inhibitor of protein phosphatases, 1 and 2A, correlates with the induction of AP1. J. Biol. Chem. 267:10810-10815.
54. Perrin, S., and G. Gilliland. 1990. Site specific mutagenesis using asymmetric polymerase chain reaction and a single mutant primer. Nucleic Acids Res. 18:7433-7438.
55. Peverali, F. A., T. Ramqvist, R. Saffrich, R. Pepperkok, V. Barone, and L. Philipson. 1994. Regulation of G1 progression by E2A and Id helix-loop-helix proteins. EMBO J. 13:4291-4301
56. Pongubala, J. M. R., and M. L. Atchison. 1991 Functional characterization of the developmentally controlled immunoglobulin kappa 3′ enhancer: regulation by Id, a repressor of helix-loop-helix transcription factors. Mol. Cell. Biol. 11:1040-1047.
57. Rauscher, F. Personal communication.
58. Riechmann, V., I. Van Cruchten, and F. Sablitzky. 1994. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucleic Acids Res. 22:749-755.
59. Safrany, G., and R. P. Perry. 1993. Characterization of the mouse gene that encodes the δ/YY1/NF-E1/UCRBP transcription factor. Proc. Natl. Acad. Sci. USA 90:5559-5563
60. Saisanit, S., and X.-H. Sun. 1995 A novel enhancer, the pro-B enhancer, regulates Id1 gene expression in progenitor B cells. Mol Cell Biol. 15:1513-1521.
61. Sartorelli, V., N. A. Hong, N. H. Bishopric, and L. Kedes. 1992 Myocardial activation of the human cardiac alpha-actin promoter by helix-loop-helix proteins. Proc. Natl. Acad Sci USA 89:4047-4051.
62. Sawada, S., and D. R. Littman. 1993. A heterodimer of HEB and an E12-related protein interacts with the CD4 enhancer and regulates its activity in T-cell lines. Mol. Cell. Biol. 13:5620-5628.
63. Shoji, W., T. Yamamoto, and M. Obinata. 1994 The helix-loop-helix protein Id inhibits differentiation of murine erythroleukemia cells. J. Biol. Chem 269:5078-5084.
64. Sleigh, M. J. 1986. A non chromatographic assay for expression of the chloramphenicol acetyltransferase gene in eucaryotic cells. Anal. Biochem. 156:251-256.
65. Sorrentino, V., R. Pepperkok, R. L. Davis, W. Ansorge, and L. Philipson. 1990. Cell proliferation inhibited by MyoD1 independently of myogenic differentiation. Nature (London) 345:813-815
66. Sukhatme, V. P. 1991. The Egr family of nuclear signal transducers. Am. J. Kidney Dis 17:615-618.
67. Sukhatme, V. P., X. Cao, L. Chang, C. H. Tsai-Morris, D. Stamenkovich, P. C. P. Ferreira, D. R. Cohen, S. A. Edwards, T. B. Shows, T. Curran, M. M. Le Beau, and E. D. Adamson. 1988. A zinc-finger encoding gene coregulated with c-fos during growth and differentiation, and after cellular depolarization. Cell 53:37-43.
68. Sukhatme, V. P., K. Sreedharan, F. G. Toback, R. Taub, R. G. Hoover, and C. H. Tsai-Morris. 1987. A novel early growth response gene rapidly induced by fibroblast, epithelial cell and lymphocyte mitogens. Oncogene Res. 1:343-355.
69. Sun, X.-H., N. G. Copeland, N. A. Jenkins, and D. Baltimore. 1991. Id proteins Id1 and Id2 selectively inhibit DNA binding by one class of helix-loop-helix proteins. Mol Cell. Biol. 11:5603-5611.
70. Tapscott, S. J., R. L. Davis, M. J. Thayer, P. F. Cheng, H. Weintraub, and A. B. Lassar. 1988 MyoD: a nuclear phosphoprotein requiring a myc homology region to convert fibroblasts to myoblasts Science 242:405-411.
71. Tietze, K., N. Oellers, and E. Knust. 1992. Enhancer of splitD, a dominant mutation of Drosophila, and its use in the study of functional domains of a helix-loop-helix protein. Proc. Natl. Acad. Sci. USA 89:6152-6156.
72. Tournay, O. 1995. Transcription of the dominant negative helix-loop-helix protein Id1 is regulated by a protein complex containing the immediate early response gene Egr-1. Ph.D. thesis University of Pennsylvania, Philadelphia.
73. Vilares, R., and C. V. Cabrera. 1987. The achaete-scute gene complex of D. melanogaster: conserved domains in a subset of genes required for neurogenesis and their homology to myc. Cell 50:415-424.
74. Wang, Y., R. Benezra, and D. Sassoon. 1992. Id expression during mouse development: a role in morphogenesis. Dev. Dyn. 194:222-230.
75. Weintraub, H. 1993. The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell 75:1241-1244.
76. Williams, T., and R. Tjian. 1991. Analysis of the DNA binding activity and activation properties of the human transcription factor AP-2. Genes Dev. 5:670-682.
77. Wilson, R. B., M. Kiledjian, C.-P. Shen, R. Benezra, P. Zwollo, S. M. Dymecki, S. V. Desiderio, and T. Kadesch. 1991. Repression of immunoglobulin enhancers by the helix-loop-helix protein Id: implications for B-lymphoid-cell development. Mol. Cell. Biol. 11:6185-6191.