Helix-Loop-Helix Proteins: Regulators of Transcription in Eucaryotic Organisms

REFERENCES

• Ahmad, I.. 1995. Mash-1 is expressed during ROD photoreceptor differentiation and binds an E-box, E opsin-1 in the rat opsin gene. Brain Res. Dev. Brain Res. 90:184–189
   PubMedGoogle Scholar
• Alani, R., Hasskarl, J., Grace, M., Hernandez, M.-C., Israel, M., and Munger, K.. 1999. Immortalization of primary human keratinocytes by the helix-loop-helix protein, Id-1. Proc. Natl. Acad. Sci. USA 96:9637–9641
   PubMedGoogle Scholar
• Alland, L., Muhle, R., Hou, H.Jr., Potes, J., Chin, L., Schreiber-Agus, N., and DePinho, R. A.. 1997. Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387:49–55
   PubMed Web of Science ®Google Scholar
• Alonso, M., and Cabrera, C.. 1988. The Achaete-Scute gene complex of Drosophila melanogaster comprises four homologous genes. EMBO 7:2585–2591
   PubMed Web of Science ®Google Scholar
• Aronheim, A., Shiran, R., Rosen, A., and Walker, M. D.. 1993. The E2A gene product contains two separable and functionally distinct transcription activation domains. Proc. Natl. Acad. Sci. USA 90:8063–8067
   PubMedGoogle Scholar
• Atchley, W., and Fitch, W.. 1997. A natural classification of the basic helix-loop-helix class of transcription factors. Proc. Natl. Acad. Sci. USA 94:5172–5176
   PubMed Web of Science ®Google Scholar
• Ayer, D., Kretzner, L., and Eisenman, R.. 1993. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72:211–222
   PubMed Web of Science ®Google Scholar
• Ayer, D., Lawrence, Q., and Eisenman, R.. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767–776
   PubMed Web of Science ®Google Scholar
• Baer, R.. 1993. TAL1, TAL2 and LYL1: a family of basic helix-loop-helix proteins implicated in T cell acute leukaemia. Semin. Cancer Biol. 4:341–347
   PubMed Web of Science ®Google Scholar
• Bain, G., Engel, I., Maandag, E. R., te Riele, H., Voland, J., Sharp, L., Chun, J., Huey, B., Pinkel, D., and Murre, C.. 1997. E2A deficiency leads to abnormalities in αβ T-cell development and to the rapid development of T-cell lymphomas. Mol. Cell. Biol. 17:4782–4791
   PubMed Web of Science ®Google Scholar
• Bain, G., Gruenwald, S., and Murre, C.. 1993. E2A and E2-2 are subunits of B-cell-specific E2-box DNA-binding proteins. Mol. Cell. Biol. 13:3522–3529
   PubMed Web of Science ®Google Scholar
• Bain, G., Maandag, E., Izon, D., Amsen, D., Kruisbeek, A., Weintraub, B., Krop, I., Schlissel, M., Feeney, A., van Roon, M., van der Valk, M., te Riele, H., Berns, A., and Murre, C.. 1994. E2A proteins are required for proper B cell development and initiation of immunoglobulin gene rearrangements. Cell 79:885–892
   PubMed Web of Science ®Google Scholar
• Bain, G., Romanow, W., Albers, K., Havran, W., and Murre, C.. 1999. Positive and negative regulation of V(D)J recombination by the E2A proteins. J. Exp. Med. 189:289–300
   PubMed Web of Science ®Google Scholar
• Bannister, A., and Kouzarides, T.. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641–643
   PubMed Web of Science ®Google Scholar
• Barbaric, S., Munsterkotter, M., Goding, C., and Horz, W.. 1998. Cooperative Pho2-Pho4 interactions at the PHO5 promoter are critical for binding of Pho4 to UASp1 and for efficient transactivation by Pho4 at UASp2. Mol. Cell. Biol. 18:2629–2639
   PubMedGoogle Scholar
• Barek, C.. 1992. The development of B cells and the B cell repertoire in the microenvironment of the germinal center. Immunol. Rev. 126:7–18
   Google Scholar
• Ben-Arie, N., Bellen, H. J., Armstrong, D. L., McCall, A. E., Gordadze, P. R., Guo, Q., Matzuk, M. M., and Zoghbi, H. Y.. 1997. Math1 is essential for genesis of cerebellar granule neurons. Nature 390:169–172
   PubMed Web of Science ®Google Scholar
• Benezra, R., Davis, R., Lockshon, D., Turner, D., and Weintraub, H.. 1990. The protein Id—a negative regulator of helix-loop-helix DNA binding proteins. Cell 61:49–59
   PubMed Web of Science ®Google Scholar
• Berben, G., Legrain, M., Gilliquet, V., and Hilger, F.. 1990. The yeast regulatory gene PHO4 encodes a helix-loop-helix motif. Yeast 6:451–454
   PubMed Web of Science ®Google Scholar
• Bermingham, N., Hassan, B., Price, S., Vollrath, M., Ben-Arie, N., Eatock, R., Bellen, H., Lysakowski, A., and Zoghbi, H.. 1999. Math1: an essential gene for the generation of inner ear hair cells. Science 284:1837–1842
   PubMed Web of Science ®Google Scholar
• Bessis, A., Salmon, A., Zoli, M., Le Novere, N., Picciotto, M., and Changeux, J.. 1995. Promoter elements conferring neuron-specific expression of the beta 2-subunit of the neuronal nicotinic acetylcholine receptor studied in vitro and in transgenic mice. Neuroscience 69:807–819
   PubMedGoogle Scholar
• Blackwood, E. M., and Eisenman, R. N.. 1991. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251:1211–1217
   PubMed Web of Science ®Google Scholar
• Bopp, D., Bell, L., Cline, T., and Schedl, P.. 1991. Developmental distribution of female-specific Sex-lethal proteins in Drosophila melanogaster. Genes Dev. 5:403–415
   PubMed Web of Science ®Google Scholar
• Braun, T., and Arnold, H. H.. 1995. Inactivation of Myf-6 and Myf-5 genes in mice leads to alterations in skeletal muscle development. EMBO J. 14:1176–1186
   PubMed Web of Science ®Google Scholar
• Braun, T., Rudnicki, M. A., Arnold, H. H., and Jaenisch, R.. 1992. Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death. Cell 71:369–382
   PubMed Web of Science ®Google Scholar
• Brown, M. S., and Goldstein, J. L.. 1997. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89:331–340
   PubMed Web of Science ®Google Scholar
• Buskin, J. N., and Hauschka, S. D.. 1989. Identification of a myocyte nuclear factor which binds to the muscle-specific enhancer of the mouse muscle creatine kinase gene. Mol. Cell. Biol. 9:2627–2640
   PubMedGoogle Scholar
• Cai, M., and Davis, R.. 1990. Yeast centromere binding protein CBF1, of the helix-loop-helix protein family, is required for chromosome stability and methionine prototrophy. Cell 61:437–446
   PubMed Web of Science ®Google Scholar
• Chen, G., Fernandez, J., Mische, S., and Courey, A.. 1999. A functional interaction between the histone deacetylase Rpd3 and the corepressor Groucho in Drosophila development. Genes Dev. 13:2218–2230
   PubMed Web of Science ®Google Scholar
• Cheng, S. W., Davies, K. P., Yung, E., Beltran, R. J., Yu, J., and Kalpana, G. V.. 1999. c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function. Nat. Genet. 22:102–105
   PubMed Web of Science ®Google Scholar
• Choi, J., Shen, C.-P., Radomska, H., Eckhardt, L., and Kadesch, T.. 1996. E47 activates the Ig-heavy chain and TdT loci in non-B cells. EMBO J. 15:5014–5021
   PubMedGoogle Scholar
• Cline, T. W.. 1989. The affairs of daughterless and the promiscuity of developmental regulators. Cell 59:231–234
   PubMed Web of Science ®Google Scholar
• Cole, M.. 1986. The myc oncogene: its role in transformation and differentiation. Annu. Rev. Gen. 20:361–385
   PubMed Web of Science ®Google Scholar
• Crews, S.. 1998. Control of cell lineage-specific development and transcription by bHLH-PAS proteins. Genes Dev. 12:607–620
   PubMed Web of Science ®Google Scholar
• Cronmiller, C., and Cline, T. W.. 1987. The sex determination gene daughterless has different functions in the germ line versus the soma. Cell 48:479–487
   PubMed Web of Science ®Google Scholar
• Deed, R., Hara, E., Atherton, G., Peters, G., and Norton, J.. 1997. Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. Mol. Cell. Biol. 17:6815–6821
   PubMedGoogle Scholar
• Eckner, R., Yao, T.-P., Oldread, E., and Livingston, D.. 1996. Interaction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation. Genes Dev. 10:2478–2490
   PubMed Web of Science ®Google Scholar
• Ellenberger, T., Fass, D., Arnaud, M., and Harrison, S.. 1994. Crystal structure of transcription factor E47: E-box recognition by a basic region helix-loop-helix dimer. Genes Dev. 8:970–980
   PubMed Web of Science ®Google Scholar
• Ellis, H. M., Spann, D. R., and Posakony, J. W.. 1990. extramacrochaetae, a negative regulator of sensory organ development in Drosophila, defines a new class of helix-loop-helix proteins. Cell 61:27–38
   PubMedGoogle Scholar
• Engel, I., and Murre, C.. 1999. Ectopic expression of E47 or E12 promotes the death of E2A-deficient lymphomas. Proc. Natl. Acad. Sci. USA 96:996–1001
   PubMedGoogle Scholar
• Ephrussi, A., Church, G. M., Tonegawa, S., and Gilbert, W.. 1985. B-lineage-specific interactions of an immunoglobulin enhancer with cellular factors in vivo. Science 227:134–140
   PubMed Web of Science ®Google Scholar
• Facchini, L., and Penn, L.. 1998. The molecular role of Myc in growth and transformation: recent discoveries lead to new insights. FASEB J. 12:633–651
   PubMed Web of Science ®Google Scholar
• Fascher, K.-D., Schmitz, J., and Horz, W.. 1993. Structural and functional requirements for the chromatin transition at the PHO5 promoter in Saccharomyces cerevisiae upon PHO5 activation. J. Mol. Biol. 231:658–667
   PubMedGoogle Scholar
• Ferre-D'Amare, A., Prendergast, G., Ziff, E., and Burley, S.. 1993. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363:38–45
   PubMed Web of Science ®Google Scholar
• Firulli, A. B., McFadden, D. G., Lin, Q., Srivastava, D., and Olson, E. N.. 1998. Heart and extra-embryonic mesodermal defects in mouse embryos lacking the bHLH transcription factor Hand1. Nat. Genet. 18:266–270
   PubMed Web of Science ®Google Scholar
• Fisher, A. L., and Caudy, M.. 1998. Groucho proteins: transcriptional corepressors for specific subsets of DNA-binding transcription factors in vertebrates and invertebrates. Genes Dev. 12:1931–1940
   PubMed Web of Science ®Google Scholar
• Garrell, J., and Modolel, J.. 1990. The Drosophila extramacrochaetae locus, an antagonist of proneural genes that like these genes, encodes a helix-loop-helix protein. Cell 61:39–48
   PubMedGoogle Scholar
• Gerber, A., Klesert, T., Bergstrom, D., and Tapscott, S.. 1997. Two domains of MyoD mediate transcriptional activation of genes in repressive chromatin: a mechanism for lineage determination in myogenesis. Genes Dev. 11:436–450
   PubMedGoogle Scholar
• German, M., Blanar, M., Nelson, C., Moss, L., and Rutter, W.. 1991. Two related helix-loop-helix proteins participate in separate cell-specific complexes that bind the insulin enhancer. Mol. Endocrinol. 5:292–299
   PubMedGoogle Scholar
• Goldfarb, A., Flores, J., and Lewandowska, K.. 1996. Involvement of the E2A basic helix-loop-helix protein in immunoglobulin heavy chain class switching. Mol. Immunol. 33:947–956
   PubMedGoogle Scholar
• Gossett, L., Kelvin, D., Sternberg, E., and Olsen, E.. 1989. A new myocyte-specific enhancer binding factor that recognizes a conserved element associated with multiple muscle-specific genes. Mol. Cell. Biol. 9:5022–5033
   PubMed Web of Science ®Google Scholar
• Grant, A., Jones, A., Thomas, K., and Wisden, W.. 1996. Characterization of the rat hippocalcin gene: the 5′ flanking region directs expression to the hippocampus. Neuroscience 75:1099–1115
   PubMedGoogle Scholar
• Grant, P., Schieltz, D., Pray-Grant, M., Steger, D., Reese, J., Yates, J.III, and Workman, J.. 1998. A subset of TAFIIs are integral components of the SAGA complex required for nucleosomal acetylation and transcription stimulation. Cell 94:45–53
   PubMedGoogle Scholar
• Grant, P., Schieltz, D., Pray-Grant, M., Yates, J.III, and Workman, J.. 1998. The ATM-related cofactor Tra1 is a component of the purified SAGA complex. Mol. Cell 2:863–867
   PubMed Web of Science ®Google Scholar
• Guillemot, F., Lo, L.-C., Johnson, J., Auerbach, A., Anderson, D., and Joyner, A.. 1993. Mammalian achaete-scute homolog 1 is required for the early development of olfactory and autonomic neurons. Cell 75:463–476
   PubMed Web of Science ®Google Scholar
• Halevy, O., Novitch, B., Spicer, D., Skapek, S., Rhee, J., Hannon, G., Beach, D., and Lassar, A.. 1995. Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD. Science 267:1018–1021
   PubMed Web of Science ®Google Scholar
• Hamamori, Y., Sartorelli, V., Ogryzko, V., Puri, P., Wu, H.-Y., Wang, J., Nakatani, Y., and Kedes, L.. 1999. Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A. Cell 96:405–413
   PubMed Web of Science ®Google Scholar
• Hamamori, Y., Wu, H.-Y., Sartorelli, V., and Kedes, L.. 1997. The basic domain of myogenic basic helix-loop-helix (bHLH) proteins is the novel target for direct inhibition by another bHLH protein, Twist. Mol. Cell. Biol. 17:6563–6573
   PubMedGoogle Scholar
• Hankinson, O.. 1995. The aryl hydrocarbon receptor complex. Annu. Rev. Pharmacol. Toxicol. 35:307–340
   PubMed Web of Science ®Google Scholar
• Hara, E., Hall, M., and Peters, G.. 1997. Cdk2-dependent phosphorylation of Id2 modulates activity of E2A-related transcription factors. EMBO J. 16:101–110
   Google Scholar
• Hasty, P., Bradley, A., Morris, J. H., Edmondson, D. G., Venuti, J. M., Olson, E. N., and Klein, W. H.. 1993. Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene. Nature 364:501–506
   PubMed Web of Science ®Google Scholar
• Heemskerk, M. H., Blom, B., Nolan, G., Stegmann, A. P., Bakker, A. Q., Weijer, K., Res, P. C., and Spits, H.. 1997. Inhibition of T cell and promotion of natural killer cell development by the dominant negative helix loop helix factor Id3. J. Exp. Med. 186:1597–1602
   PubMed Web of Science ®Google Scholar
• Heinzel, T., Lavinsky, R. M., Mullen, T. M., Söderstrom, M., Laherty, C. D., Torchia, J., Yang, W. M., Brard, G., Ngo, S. D., Davie, J. R., Seto, E., Eisenman, R. N., Rose, D. W., Glass, C. K., and Rosenfeld, M. G.. 1997. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387:43–48
   PubMed Web of Science ®Google Scholar
• Henriksson, M., and Luscher, B.. 1996. Proteins of the Myc network: essential regulators of cell growth and differentiation. Adv. Cancer Res. 68:109–182
   PubMed Web of Science ®Google Scholar
• Henthorn, P., Kiledjian, M., and Kadesch, T.. 1990. Two distinct transcription factors that bind the immunoglobulin enhancer μE5/ κE2 motif. Science 247:467–470
   PubMed Web of Science ®Google Scholar
• Henthorn, P., Stewart, C., Kadesch, T., and Puck, J.. 1991. The gene encoding human TFE3, a transcription factor that binds the immunoglobulin heavy-chain enhancer, maps to xp11;22. Genomics 11:374–378
   PubMed Web of Science ®Google Scholar
• Hoshizaki, D., Hill, J., and Henry, S.. 1990. The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes. J. Biol. Chem. 265:3320–3328
   PubMedGoogle Scholar
• Hua, X., Liu, X., Ansari, D., and Lodish, H.. 1998. Synergistic cooperation of TFE3 and Smad proteins in TGF-β-induced transcription of the plasminogen activator inhibitor-1 gene. Genes Dev. 12:3084–3095
   PubMed Web of Science ®Google Scholar
• Iavarone, A., Garg, P., Lasorella, A., Hsu, J., and Israel, M.. 1994. The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein. Genes Dev. 8:1270–1284
   PubMedGoogle Scholar
• Ishibashi, M., Ang, S. L., Shiota, K., Nakanishi, S., Kageyama, R., and Guillemot, F.. 1995. Targeted disruption of mammalian hairy and Enhancer of split homolog-1 (HES-1) leads to up-regulation of neural helix-loop-helix factors, premature neurogenesis, and severe neural tube defects. Genes Dev. 9:3136–3148
   PubMed Web of Science ®Google Scholar
• Jain, S., Dolwick, K., Schmidt, J., and Bradfield, C.. 1994. Potent transactivation domains of the Ah receptor and the Ah receptor nuclear translocator map to their carboxy termini. J. Biol. Chem. 269:31518–31524
   PubMed Web of Science ®Google Scholar
• Jen, Y., Manova, K., and Benezra, R.. 1997. Each member of the Id gene family exhibits a unique expression pattern in mouse gastrulation and neurogenesis. Dev. Dyn. 208:92–106
   PubMed Web of Science ®Google Scholar
• Jia, Y., Rothermel, B., Thornton, J., and Butow, R.. 1997. A basic helix-loop-helix-leucine zipper transcription complex in yeast functions in a signaling pathway from mitochondria to the nucleus. Mol. Cell. Biol. 17:1110–1117
   PubMed Web of Science ®Google Scholar
• Kee, B., and Murre, C.. 1998. Induction of early B cell factor (EBF) and multiple B lineage genes by the basic helix-loop-helix transcription factor E12. J. Exp. Med. 188:699–713
   PubMedGoogle Scholar
• Keyes, L., Cline, T., and Schedl, P.. 1992. The primary sex determination signal of Drosophila acts at the level of transcription. Cell 68:933–943
   PubMedGoogle Scholar
• Klambt, C., Knust, E., Tietze, K., and Campos-Ortega, J. A.. 1989. Closely related transcripts encoded by the neurogenic gene complex enhancer of split of Drosophila melanogaster. EMBO J. 8:203–210
   PubMed Web of Science ®Google Scholar
• Kleeff, J., Ishiwata, T., Friess, H., Buchler, M., Israel, M., and Korc, M.. 1998. The helix-loop-helix protein Id2 is overexpressed in human pancreatic cancer. Cancer Res. 58:3769–3772
   PubMedGoogle Scholar
• Ko, H., Okino, S., Ma, Q., Whitlock, J.Jr.. 1996. Dioxin-induced CYP1A1 transcription in vivo: the aromatic hydrocarbon receptor mediates transactivation, enhancer-promoter communication, and changes in chromatin structure. Mol. Cell. Biol. 16:430–436
   PubMed Web of Science ®Google Scholar
• Ko, H., Okino, S., Ma, Q., Whitlock, J.Jr.. 1997. Transactivation domains facilitate promoter occupancy for the dioxin-inducible CYP1A1 gene in vivo. Mol. Cell. Biol. 17:3497–3507
   PubMed Web of Science ®Google Scholar
• Komeili, A., and O'Shea, E.. 1999. Roles of phosphorylation sites in regulating activity of the transcription factor Pho4. Science 284:977–980
   PubMed Web of Science ®Google Scholar
• Krause, M., Park, M., Zhang, J. M., Yuan, J., Harfe, B., Xu, S. Q., Greenwald, I., Cole, M., Paterson, B., and Fire, A.. 1997. A C. elegans E/Daughterless bHLH protein marks neuronal but not striated muscle development. Development 124:2179–89
   PubMed Web of Science ®Google Scholar
• Laherty, C. D., Yang, W. M., Sun, J. M., Davie, J. R., Seto, E., and Eisenman, R. N.. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89:349–356
   PubMed Web of Science ®Google Scholar
• Langlands, K., Yin, X., Anand, G., and Prochownik, E. V.. 1997. Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. 272:19785–19793
   PubMedGoogle Scholar
• Larson, R. C., Lavenir, I., Larson, T. A., Baer, R., Warren, A. J., Wadman, I., Nottage, K., and Rabbitts, T. H.. 1996. Protein dimerization between Lmo2(Rbtn2) and Tal1 alters thymocyte development and potentiates T cell tumorigenesis in transgenic mice. EMBO J. 15:1021–1027
   PubMed Web of Science ®Google Scholar
• Lassar, A. B., Buskin, J. N., Lockshon, D., Davis, R. L., Apone, S., Hauschka, S. D., and Weintraub, H.. 1989. MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer. Cell 58:823–831
   PubMedGoogle Scholar
• Lee, J. E., Hollenberg, S. M., Snider, L., Turner, D. L., Lipnick, N., and Weintraub, H.. 1995. Conversion of Xenopus ectoderm into neurons by neuroD, a basic helix-loop-helix protein. Science 268:836–844
   PubMed Web of Science ®Google Scholar
• Lemercier, C., To, R. Q., Carrasco, R. A., and Konieczny, S. F.. 1998. The basic helix-loop-helix transcription factor Mist1 functions as a transcriptional repressor of MyoD. EMBO J. 17:1412–1422
   PubMed Web of Science ®Google Scholar
• Lenburg, M. E., and O'Shea, E. K.. 1996. Signaling phosphate starvation. Trends Biochem. Sci. 21:383–387
   PubMedGoogle Scholar
• Liao, X., and Butow, R.. 1993. RTG1 and RTG2: two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 72:61–71
   PubMed Web of Science ®Google Scholar
• Liao, X., Small, W., Srere, P., and Butow, R.. 1991. Intramitochondrial functions regulate nonmitochondrial citrate synthase (CIT2) expression in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:38–46
   PubMedGoogle Scholar
• Luger, K., Mader, A., Richmond, R., Sargent, D., and Richmond, T.. 1997. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389:251–260
   PubMed Web of Science ®Google Scholar
• Lyden, D., Young, A., Zagzag, D., Yan, W., Gerald, W., O'Reilly, R., Bader, B., Hynes, R., Zhuang, Y., Manova, K., and Benezra, R.. 1999. Id1 and Id3 are required for neurogenesis, angiogenesis and vascularization of tumor xenografts. Nature 401:670–677
   PubMed Web of Science ®Google Scholar
• Ma, Q., Chen, Z., del Barco Barrantes, I., de la Pompa, J. L., and Anderson, D. J.. 1998. Neurogenin1 is essential for the determination of neuronal precursors for proximal cranial sensory ganglia. Neuron 20:469–482
   PubMed Web of Science ®Google Scholar
• Ma, Q., Kintner, C., and Anderson, D. J.. 1996. Identification of neurogenin, a vertebrate neuronal determination gene. Cell 87:43–52
   PubMed Web of Science ®Google Scholar
• Martinsen, B. J., and Bronner-Fraser, M.. 1998. Neural crest specification regulated by the helix-loop-helix repressor Id2. Science 281:988–991
   PubMed Web of Science ®Google Scholar
• Massari, M., Grant, P., Pray-Grant, M., Berger, S., Workman, J., and Murre, C.. 1999. A conserved motif present in a class of helix-loop-helix proteins activates transcription by direct recruitment of the SAGA complex. Mol. Cell 4:63–73
   PubMed Web of Science ®Google Scholar
• Massari, M., Jennings, P., and Murre, C.. 1996. The AD1 transactivation domain of E2A contains a highly conserved helix which is required for its activity in both Saccharomyces cerevisiae and mammalian cells. Mol. Cell. Biol. 16:121–129
   PubMedGoogle Scholar
• Massari, M., Rivera, R., Voland, J., Quong, M., Breit, T., van Dongen, J., de Smit, O., and Murre, C.. 1998. Characterization of ABF-1, a novel basic helix-loop-helix transcription factor expressed in activated B lymphocytes. Mol. Cell. Biol. 18:3130–3139
   PubMedGoogle Scholar
• McMahon, S. B., Van Buskirk, H. A., Dugan, K. A., Copeland, T. D., and Cole, M. D.. 1998. The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins. Cell 94:363–374
   PubMed Web of Science ®Google Scholar
• Morrow, M., Mayer E., Perez C., Adlam M., and Siu G.. Overexpression of the helix-loop-helix protein Id2 blocks T cell development at multiple stages. Mol. Immunol., in press.
   Google Scholar
• Murre, C., Bain, G., Dijk, M. A. v., Engel, I., Furnari, B. A., Massari, M. E., Matthews, J. R., Quong, M. W., Rivera, R. R., and Stuiver, M. H.. 1994. Structure and function of helix-loop-helix proteins. Biochim. Biophys. Acta 1218:129–135
   PubMed Web of Science ®Google Scholar
• Murre, C., McCaw, P. S., and Baltimore, D.. 1989. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell 56:777–783
   PubMed Web of Science ®Google Scholar
• Murre, C., Mccaw, P. S., Vaessin, H., Caudy, M., Jan, L. Y., Jan, Y. N., Cabrera, C. V., Buskin, J. N., Hauschka, S. D., Lassar, A. B., Weintraub, H., and Baltimore, D.. 1989. Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence. Cell 58:537–544
   PubMed Web of Science ®Google Scholar
• Murre, C., Voronova, A., and Baltimore, D.. 1991. B-cell- and myocyte-specific E2-box-binding factors contain E12/E47-like subunits. Mol. Cell. Biol. 11:1156–1160
   PubMedGoogle Scholar
• Mutoh, H., Naya, F., Tsai, M.-J., and Leiter, A.. 1998. The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate differentiation of secretin-expressing enteroendocrine cells. Genes Dev. 12:820–830
   PubMedGoogle Scholar
• Naar, A., Beaurang, P., Robinson, K., Oliner, J., Avizonis, D., Scheek, S., Zwicker, J., Kadonaga, J., and Tjian, R.. 1998. Chromatin, TAFs, and a novel multiprotein coactivator are required for synergic activation by Sp1 and SREBP-1a in vitro. Genes Dev. 12:3020–3031
   PubMed Web of Science ®Google Scholar
• Nabeshima, Y., Hanaoka, K., Hayasaka, M., Esumi, E., Li, S., Nonaka, I., and Nabeshima, Y.. 1993. Myogenin gene disruption results in perinatal lethality because of severe muscle defects. Nature 364:532–535
   PubMed Web of Science ®Google Scholar
• Naya, F., Huang, H.-P., Qiu, Y., Mutoh, H., DeMayo, F., Leiter, A., and Tsai, M.-J.. 1997. Diabetes, defective pancreatic morphogenesis, and abnormal enteroendocrine differentiation in BETA2/NeuroD-deficient mice. Genes Dev. 11:2323–2334
   PubMed Web of Science ®Google Scholar
• Nelsen, B., and Sen, R.. 1992. Regulation of immunoglobulin gene transcription. Int. Rev. Cytol. 133:121–149
   PubMedGoogle Scholar
• Nelsen, B., Tian, G., Erman, B., Gregoire, J., Maki, R., Graves, B., and Sen, R.. 1993. Regulation of the lymphoid-specific immunoglobulin mu heavy chain gene enhancer by the ETS-domain proteins. Science 261:82–86
   PubMed Web of Science ®Google Scholar
• Nelson, C., Shen, L. P., Meister, A., Fodor, E., and Rutter, W. J.. 1990. Pan: a transcriptional regulator that binds chymotrypsin, insulin and AP-4 enhancer motifs. Genes Dev. 4:1035–1044
   PubMedGoogle Scholar
• Nikoloff, D., McGraw, P., and Henry, S.. 1992. The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis. Nucleic Acids Res. 20: 3253
   PubMedGoogle Scholar
• Ogryzko, V., Kotani, T., Zhang, X., Schlitz, R., Howard, T., Yang, X., Howard, B., Qin, J., and Nakatani, Y.. 1998. Histone-like TAFs within the PCAF histone acetylase complex. Cell 94:35–44
   PubMedGoogle Scholar
• Ogryzko, V., Schiltz, R., Russanova, V., Howard, B., and Nakatani, Y.. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959
   PubMed Web of Science ®Google Scholar
• Olson, E.. 1990. MyoD family: a paradigm for development? Genes Dev. 4:1454–1461
   PubMed Web of Science ®Google Scholar
• Olson, E. N., Arnold, H. H., Rigby, P. W., and Wold, B. J.. 1996. Know your neighbors: three phenotypes in null mutants of the myogenic bHLH gene MRF4. Cell 85:1–4
   PubMed Web of Science ®Google Scholar
• Ono, Y., Fukuhara, N., and Yoshie, O.. 1998. TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3. Mol. Cell. Biol. 18:6939–6950
   PubMedGoogle Scholar
• O'Riordan, M., and Grosschedl, R.. 1997. EBF and E47 collaborate to induce expression of the endogenous immunoglobulin surrogate light chain genes. Immunity 7:25–36
   PubMedGoogle Scholar
• Park, C., and Walker, M.. 1992. Subunit structure of cell-specific E-box binding proteins analyzed by quantitation of electrophoretic mobility shift. J. Biol. Chem. 267:15642–15649
   PubMedGoogle Scholar
• Park, S. T., Nolan, G. P., and Sun, X. H.. 1999. Growth inhibition and apoptosis due to restoration of E2A activity in T cell acute lymphoblastic leukemia cells. J. Exp. Med. 189:501–508
   PubMedGoogle Scholar
• Park, S. T., and Sun, X. H.. 1998. The Tal1 oncoprotein inhibits E47-mediated transcription. Mechanism of inhibition. J. Biol. Chem. 273:7030–7037
   PubMedGoogle Scholar
• Parkhurst, S., and Meneely, P.. 1994. Sex determination and dosage compensation: lessons from flies and worms. Science 264:924–932
   PubMedGoogle Scholar
• Parkhurst, S. M.. 1998. Groucho: making its Marx as a transcriptional co-repressor. Trends Genet. 14:130–132
   PubMedGoogle Scholar
• Patapoutian, A., Yoon, J. K., Miner, J. H., Wang, S., Stark, K., and Wold, B.. 1995. Disruption of the mouse MRF4 gene identifies multiple waves of myogenesis in the myotome. Development 121:3347–3358
   PubMed Web of Science ®Google Scholar
• Pepitoni, S., Wood, I., and Buckley, N.. 1997. Structure of the m1 muscarinic acetylcholine receptor gene and its promoter. J. Biol. Chem. 272:17112–17117
   PubMedGoogle Scholar
• Peverali, F., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M., and Philipson, L.. 1994. Regulation of G1 progression by E2A and Id helix-loop-helix proteins. EMBO J. 13:4291–4301
   PubMedGoogle Scholar
• Porcher, C., Swat, W., Rockwell, K., Fujiwara, Y., Alt, F., and Orkin, S.. 1996. The T cell leukemia oncoprotein SCL/tal-1 is essential for development of all hematopoietic lineages. Cell 86:47–57
   PubMed Web of Science ®Google Scholar
• Prabhu, S., Ignatova, A., Park, S., and Sun, X.-H.. 1997. Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins. Mol. Cell. Biol. 17:5888–5896
   PubMedGoogle Scholar
• Puri, P., Sartorelli, V., Yang, X.-J., Hamamori, Y., Ogryzko, V., Howard, B., Kedes, L., Wang, J., Graessmann, A., Nakatani, Y., and Levrero, M.. 1997. Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol. Cell. 1:35–45
   PubMed Web of Science ®Google Scholar
• Qiu, Y., Sharma, A., and Stein, R.. 1998. p300 mediates transcriptional stimulation by the basic helix-loop-helix activators of the insulin gene. Mol. Cell. Biol. 18:2957–2964
   PubMed Web of Science ®Google Scholar
• Quong, M., Harris, D., Swain, S., and Murre, C.. 1999. E2A activity is induced during B-cell activation to promote immunoglobulin class switch recombination. EMBO J. 18:6307–6318
   PubMedGoogle Scholar
• Quong, M. W., Massari, M. E., Zwart, R., and Murre, C.. 1993. A new transcriptional activation motif restricted to a class of helix-loop-helix proteins is functionally conserved in both yeast and mammalian cells. Mol. Cell. Biol. 13:792–800
   PubMedGoogle Scholar
• Riechmann, V., Cruchten, I. v., and Sablitzky, F.. 1994. The expression pattern of Id4, a novel dominant negative helix-loop-helix protein, is distinct from Id1, Id2 and Id3. Nucl. Acids Res. 22:749–755
   PubMed Web of Science ®Google Scholar
• Riechmann, V., and Sablitzky, F.. 1995. Mutually exclusive expression of two dominant-negative helix-loop-helix (dnHLH) genes, Id4 and Id3, in the developing brain of the mouse suggests distinct regulatory roles of these dnHLH proteins during cellular proliferation and differentiation of the nervous system. Cell Growth and Differentiation 6:837–43
   PubMedGoogle Scholar
• Riley, P., Anson-Cartwright, L., and Cross, J. C.. 1998. The Hand1 bHLH transcription factor is essential for placentation and cardiac morphogenesis. Nature Genetics 18:271–5
   PubMed Web of Science ®Google Scholar
• Roberts, V. J., Steenbergen, R., and Murre, C.. 1993. Localization of E2A mRNA expression in developing and adult rat tissues. Proc. Natl. Acad. Sci. USA 90:7583–7587
   PubMedGoogle Scholar
• Rothermel, B., Thornton, J., and Butow, R.. 1997. Rtg3p, a basic helix-loop-helix/leucine zipper protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains. J. Biol. Chem. 272:19801–19807
   PubMed Web of Science ®Google Scholar
• Rudnicki, M., Braun, T., Hinuma, S., and Jaenisch, R.. 1992. Inactivation of MyoD in mice leads to an up-regulation of the myogenic HLH gene Myf5 and results in apparently normal muscle development. Cell 71:383–390
   PubMed Web of Science ®Google Scholar
• Rudnicki, M., Schnegelsbery, P., Stead, R., Braun, T., Arnold, H., and Jaenisch, R.. 1993. MyoD or Myf5 is required for the formation of skeletal muscle. Cell 75:1351–1359
   PubMed Web of Science ®Google Scholar
• Rudolph, H., and Hinnen, A.. 1987. The yeast PHO5 promoter: phosphate-control elements and sequences mediating mRNA start-site selection. Proc. Natl. Acad. Sci. USA 84:1340–1344
   PubMedGoogle Scholar
• Rushlow, C. A., Hogan, A., Pinchin, S. M., Howe, K. M., Lardelli, M., and Ish-Horowicz, D.. 1989. The Drosophila hairy protein acts in both segmentation and bristle patterning and shows homology to N-myc. EMBO J. 8:3095–3103
   PubMedGoogle Scholar
• Ruvkun, G., and Hobert, O.. 1998. The taxonomy of developmental control in Caenorhabditis elegans. Science 282:2033–2041
   PubMedGoogle Scholar
• Sanchez, H. B., Yieh, L., and Osborne, T. F.. 1995. Cooperation by sterol regulatory element-binding protein and Sp1 in sterol regulation of low density lipoprotein receptor gene. J. Biol. Chem. 270:1161–1169
   PubMed Web of Science ®Google Scholar
• Sánchez-García, I., and Rabbitts, T.. 1993. LIM domain proteins in leukaemia and development. Semin. Cancer Biol. 4:349–358
   PubMed Web of Science ®Google Scholar
• Sartorelli, V., Huang, J., Hamamori, Y., and Kedes, L.. 1997. Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol. Cell. Biol. 17:1010–1026
   PubMed Web of Science ®Google Scholar
• Schlissel, M., Voronova, A., and Baltimore, D.. 1991. Helix loop helix transcription factor-E47 activates germ-line immunoglobulin heavy-chain gene transcription and rearrangement in a pre-T-cell line. Genes Dev. 5:1367–1376
   PubMedGoogle Scholar
• Schreiber-Argus, N., Chin, L., Chen, K., Torres, R., Rao, G., Guida, P., Skoultchi, A., and DePinho, R.. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80:777–786
   PubMedGoogle Scholar
• Schreiber-Argus, N., and DePinho, R.. 1998. Repression by the Mad(Mxi1)-Sin3 complex. Bioessays 20:808–818
   PubMedGoogle Scholar
• Shen, C. P., and Kadesch, T.. 1995. B-cell-specific DNA binding by an E47 homodimer. Mol. Cell. Biol. 15:4518–4524
   PubMedGoogle Scholar
• Shieh, S.-Y., and Tsai, M.-J.. 1991. Cell-specific and ubiquitous factors are responsible for the enhancer activity of the rat insulin II gene. J. Biol. Chem. 266:16707–16714
   Google Scholar
• Shivdasani, R., Mayer, E., and Orkin, S.. 1995. Absence of blood formation in mice lacking the T-cell leukaemia oncoprotein tal-1/SCL. Nature 373:432–434
   PubMed Web of Science ®Google Scholar
• Sigvardsson, M., O'Riordan, M., and Grosschedl, R.. 1997. EBF and E47 collaborate to induce expression of the endogenous immunoglobulin surrogate light chain genes. Immunity 7:25–36
   PubMed Web of Science ®Google Scholar
• Spicer, D., Rhee, J., Cheung, W., and Lassar, A.. 1996. Inhibition of myogenic bHLH and MEF2 transcription factors by the bHLH protein twist. Science 272:1476–1480
   PubMed Web of Science ®Google Scholar
• Srivastava, D., Cserjesi, P., and Olson, E. N.. 1995. A subclass of bHLH proteins required for cardiac morphogenesis. Science 270:1995–1999
   PubMedGoogle Scholar
• Srivastava, D., Thomas, T., Lin, Q., Kirby, M. L., Brown, D., and Olson, E. N.. 1997. Regulation of cardiac mesodermal and neural crest development by the bHLH transcription factor, dHAND. Nat. Genet. 16:154–160
   PubMedGoogle Scholar
• Staudt, L., and Lenardo, M.. 1991. Immunoglobulin gene transcription. Annu. Rev. Immunol. 9:373–398
   PubMed Web of Science ®Google Scholar
• Sun, X.-H., and Baltimore, D.. 1991. An inhibitory domain of E12 transcription factor prevents DNA binding in E12 homodimers but not in E12 heterodimers. Cell 64:459–470
   PubMed Web of Science ®Google Scholar
• Svaren, J., and Hörz, W.. 1997. Transcription factors vs nucleosomes: regulation of the PHO5 promoter in yeast. Trends Biochem. Sci. 22:93–97
   PubMedGoogle Scholar
• Svaren, J., Schmitz, J., and Horz, W.. 1994. The transactivation domain of Pho4 is required for nucleosome disruption at the PHO5 promoter. EMBO J. 13:4856–4862
   PubMedGoogle Scholar
• Thompson, J., Higgins, D., and Gibson, T.. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673–4680
   PubMed Web of Science ®Google Scholar
• Van Doren, M., Ellis, H., and Posakony, J.. 1991. The Drosophila extramacrochaete protein antogonizes sequence-specific DNA binding by daughterless/achaete-scute protein complexes. Development 113:245–255
   PubMedGoogle Scholar
• Vassilev, A., Yamauchi, J., Kotani, T., Prives, C., Avantaggiati, M. L., Qin, J., and Nakatani, Y.. 1998. The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily. Mol. Cell 2:869–875
   PubMedGoogle Scholar
• Venter, U., Svaren, J., Schmitz, J., Schmid, A., and Horz, W.. 1994. A nucleosome precludes binding of the transcription factor Pho4 in vivo to a critical target site in the PHO5 promoter. EMBO J. 13:4848–4855
   PubMedGoogle Scholar
• Venuti, J., and Cserjesi, P.. 1996. Molecular embryology of skeletal myogenesis. Curr. Topics Dev. Biol. 34:169–206
   PubMedGoogle Scholar
• Wadman, I. A., Osada, H., Grütz, G. G., Agulnick, A. D., Westphal, H., Forster, A., and Rabbitts, T. H.. 1997. The LIM-only protein Lmo2 is a bridging molecule assembling an erythroid, DNA-binding complex which includes the TAL1, E47, GATA-1 and Ldb1/NLI proteins. EMBO J. 16:3145–3157
   PubMed Web of Science ®Google Scholar
• Warren, A., Colledge, W., Carlton, M., Evans, M., Smith, A., and Rabbitts, T.. 1994. The oncogenic cysteine-rich LIM domain protein rbtn2 is essential for erythroid development. Cell 78:45–57
   PubMed Web of Science ®Google Scholar
• Weintraub, H., Dwarki, V., Verma, I., Davis, R., Hollenberg, S., Snider, L., Lassar, A., and Tapscott, S.. 1991. Muscle-specific transcriptional activation by MyoD. Genes Dev. 5:1377–1386
   PubMed Web of Science ®Google Scholar
• Whelan, J., Cordle, S. R., Henderson, E., Weil, P. A., and Stein, R.. 1990. Identification of a pancreatic β-cell insulin gene transcription factor that binds to and appears to activate cell-type-specific gene expression: its possible relationship to other cellular factors that bind to a common insulin gene sequence. Mol. Cell. Biol. 10:1564–1572
   PubMedGoogle Scholar
• Wrischnik, L. A., and Kenyon, C. J.. 1997. The role of lin-22, a hairy/enhancer of split homolog, in patterning the peripheral nervous system of C. elegans. Development 124:2875–2888
   PubMedGoogle Scholar
• Yamada, Y., Warren, A. J., Dobson, C., Forster, A., Pannell, R., and Rabbitts, T. H.. 1998. The T cell leukemia LIM protein Lmo2 is necessary for adult mouse hematopoiesis. Proc. Natl. Acad. Sci. USA 95:3890–3895
   PubMed Web of Science ®Google Scholar
• Yan, W., Young, A. Z., Soares, V. C., Kelley, R., Benezra, R., and Zhuang, Y.. 1997. High incidence of T-cell tumors in E2A-null mice and E2A/Id1 double-knockout mice. Mol. Cell. Biol. 17:7317–7327
   PubMedGoogle Scholar
• Yang, X.-J., Ogryzko, V., Nishikawa, J., Howard, B., and Nakatani, Y.. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319–324
   PubMed Web of Science ®Google Scholar
• Yokota, Y., Mansouri, A., Mori, S., Sugawara, S., Adachi, S., Nishikawa, S., and Gruss, P.. 1999. Development of peripheral lymphoid organs and natural killer cells depends on the helix-loop-helix inhibitor Id2. Nature 397:702–706
   PubMed Web of Science ®Google Scholar
• Zervos, A., Gyuris, J., and Brent, R.. 1994. Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell 79:388–398
   PubMedGoogle Scholar
• Zhang, W., Behringer, R. R., and Olson, E. N.. 1995. Inactivation of the myogenic bHLH gene MRF4 results in up-regulation of myogenin and rib anomalies. Genes Dev. 9:1388–1399
   PubMed Web of Science ®Google Scholar
• Zhao, C., and Emmons, S. W.. 1995. A transcription factor controlling development of peripheral sense organs in C. elegans. Nature 373:74–78
   PubMedGoogle Scholar
• Zhao, Q., Zhou, X., and Mattei, M.. 1993. TFEC, a basic helix-loop-helix protein, forms heterodimers with TFE3 and inhibits TFE3-dependent transcription activation. Mol. Cell. Biol. 13:4505–4512
   PubMed Web of Science ®Google Scholar
• Zhuang, Y., Cheng, P., and Weintraub, H.. 1996. B-lymphocyte development is regulated by the combined dosage of three basic helix-loop-helix genes, E2A, E2-2, and HEB. Mol. Cell. Biol. 16:2898–2905
   PubMed Web of Science ®Google Scholar
• Zhuang, Y., Soriano, P., and Weintraub, H.. 1994. The helix-loop-helix gene E2A is required for B cell formation. Cell 79:875–884
   PubMedGoogle Scholar