16
Views
294
CrossRef citations to date
0
Altmetric
Transcriptional Regulation

Redox-Regulated Recruitment of the Transcriptional Coactivators CREB-Binding Protein and SRC-1 to Hypoxia-Inducible Factor 1α

, , , , &
Pages 402-415 | Received 29 Mar 1999, Accepted 14 Sep 1999, Published online: 28 Mar 2023

REFERENCES

  • Antonsson, C., Arulampalam, V., Whitelaw, M. L., Pettersson, S., and Poellinger, L.. 1995. Constitutive function of the basic helix-loop-helix/PAS factor Arnt. Regulation of target promoters via the E box motif. J. Biol. Chem. 270:13968–13972
  • Anzick, S. L., Kononen, J., Walker, R. L., Azorsa, D. O., Tanner, M. M., Guan, X.-Y., Sauter, G., Kallioniemi, O.-P., Trent, J. M., and Meltzer, P. S.. 1997. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277:965–968
  • Arany, Z., Sellers, W. R., Livingston, D. M., and Eckner, R.. 1994. E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators. Cell 77:799–800
  • Arany, Z., Newsome, D., Oldread, E., Livingston, D. M., and Eckner, R.. 1995. A family of transcriptional adaptor proteins targeted by the E1A oncoprotein. Nature 374:81–84
  • Arany, Z., Huang, L. E., Eckner, R., Bhattacharya, S., Jiang, C., Goldberg, M. A., Bunn, H. F., and Livingston, D. M.. 1996. An essential role for p300/CBP in the cellular response to hypoxia. Proc. Natl. Acad. Sci. USA 93:12969–12973
  • Bannister, A. J., and Kouzarides, T.. 1996. The CBP co-activator is a histone acetyltransferase. Nature 384:641–643
  • Bhattacharya, S., Michels, C. L., Leung, M.-K., Arany, Z. P., Kung, A. L., and Livingston, D. M.. 1999. Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev. 13:64–75
  • Bunn, H. F., and Poyton, R. O.. 1996. Oxygen sensing and molecular adaptation to hypoxia. Physiol. Rev. 76:839–885
  • Chatton, B., Bahr, A., Acker, J., and Kedinger, C.. 1995. Eukaryotic GST fusion vector for the study of protein-protein associations in vivo: application to interaction of ATFa with Jun and Fos. BioTechniques 18:142–145
  • Chen, H., Lin, R. J., Schiltz, R. L., Chakravarti, D., Nash, A., Nagy, L., Privalsky, M. L., Nakatani, Y., and Evans, R. M.. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569–580
  • Eckner, R., Ewen, M. E., Newsome, D., Gerdes, M., DeCaprio, J. A., Lawrence, J. B., and Livingston, D. M.. 1994. Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:869–884
  • Eguchi, H., Ikuta, T., Tachibana, T., Yoneda, Y., and Kawajiri, K.. 1997. A nuclear localization signal of human aryl hydrocarbon receptor nuclear translocator/hypoxia-inducible factor 1 is a novel bipartite type recognized by the two components of nuclear pore-targeting complex. J. Biol. Chem. 272:17640–17647
  • Ema, M., Hirota, K., Mimura, J., Abe, H., Yodoi, J., Sogawa, K., Poellinger, L., and Fujii-Kuriyama, Y.. 1999. Molecular mechanisms of transcription activation by HLF and HIF-1α in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 18:1905–1914
  • Gradin, K., McGuire, J., Wenger, R. H., Kvietikova, I., Whitelaw, M. L., Toftgård, R., Tora, L., Gassmann, M., and Poellinger, L.. 1996. Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor. Mol. Cell. Biol. 16:5221–5231
  • Hanstein, B., Eckner, R., DiRenzo, J., Halachmi, S., Liu, H., Searcy, B., Kurokawa, R., and Brown, M.. 1996. p300 is a component of an oestrogen receptor coactivator complex. Proc. Natl. Acad. Sci. USA 93:11540–11545
  • Heery, D. M., Kalkhoven, E., Hoare, S., and Parker, M. G.. 1997. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387:733–736
  • Hong, H., Kohli, K., Trivedi, A., Johnson, D. L., and Stallcup, M. R.. 1996. GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93:4948–4952
  • Hong, H., Kohli, K., Garabedian, M. J., and Stallcup, M. R.. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735–2744
  • Hong, H., Darimont, B. D., Ma, H., Yang, L., Yamamoto, K. R., and Stallcup, M. R.. 1999. An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors. J. Biol. Chem. 274:3496–3502
  • Huang, L. E., Arany, Z., Livingston, D. M., and Bunn, H. F.. 1996. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its α subunit. J. Biol. Chem. 271:32253–32259
  • Huang, L. E., Gu, J., Schau, M., and Bunn, H. F.. 1998. Regulation of hypoxia-inducible factor 1α is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. USA 95:7987–7992
  • Jayaraman, L., Murthy, K. G. K., Zhu, C., Curran, T., Xanthoudakis, S., and Prives, C.. 1997. Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Dev. 11:558–570
  • Jiang, B.-H., Zheng, J. Z., Leung, S. W., Roe, R., and Semenza, G. L.. 1997. Transactivation and inhibitory domains of hypoxia-inducible factor 1α. J. Biol. Chem. 272:19253–19260
  • Kalkhoven, E., Valentine, J. E., Heery, D. M., and Parker, M. G.. 1998. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17:232–243
  • Kallio, P. J., Pongratz, I., Gradin, K., McGuire, J., and Poellinger, L.. 1997. Activation of hypoxia-inducible factor 1α: posttranscriptional regulation and conformational change by recruitment of the Arnt transcription factor. Proc. Natl. Acad. Sci. USA 94:5667–5672
  • Kallio, P. J., Okamoto, K., O'Brien, S., Carrero, P., Makino, Y., Tanaka, H., and Poellinger, L.. 1998. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α. EMBO J. 17:6573–6586
  • Kallio, P. J., Wilson, W. J., O'Brien, S., Makino, Y., and Poellinger, L.. 1999. Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway. J. Biol. Chem. 274:6519–6525
  • Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., and Rosenfeld, M. G.. 1996. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85:403–414
  • Kee, B. I., Arias, J., and Montminy, M. R.. 1996. Adaptor-mediated recruitment of RNA polymerase II to a signal-dependent activator. J. Biol. Chem. 271:2373–2375
  • Kobayashi, A., Numayama-Tsuruta, K., Sogawa, K., and Fujii-Kuriyama, Y.. 1997. CBP/p300 functions as a possible transcriptional coactivator of Ah receptor nuclear translocator (Arnt). J. Biochem. 122:703–710
  • Korzus, E., Torchia, J., Rose, D. W., Xu, L., Kurokawa, R., McInerney, E. M., Mullen, T.-M., Glass, C. K., and Rosenfeld, M. G.. 1998. Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science 279:703–707
  • Kwok, R. P. S., Lundland, J. R., Chrivia, J. C., Richards, J. P., Bachinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., and Goodman, R. H.. 1994. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370:223–226
  • Li, H., Gomes, P. J., and Chen, J. D.. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479–8484
  • Lindebro, M. C., Poellinger, L., and Whitelaw, M. L.. 1995. Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. EMBO J. 14:3528–3539
  • Littlewood, T. D., and Evan, G. I.. 1995. Transcription factors 2: helix-loop-helix. Protein Profile 2:621–702
  • Lundblad, J. R., Kwok, R. P., Laurance, M. E., Harter, M. L., and Goodman, R. H.. 1995. Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP. Nature 374:85–88
  • Martinez-Balbas, M. A., Bannister, A. J., Martin, K., Haus-Seuffert, P., Meisterernst, M., and Kouzarides, T.. 1998. The acetyltransferase activity of CBP stimulates transcription. EMBO J. 17:2886–2893
  • McInerney, E. M., Rose, D. W., Flynn, S. E., Westin, S., Mullen, T.-M., Krones, A., Inostroza, J., Torchia, J., Nolte, R. T., Assa-Munt, N., Milburn, M. V., Glass, C. K., and Rosenfeld, M. G.. 1998. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:3357–3368
  • Na, S. Y., Lee, S. K., Han, S. J., Choi, H. S., Im, S. Y., and Lee, J. W.. 1998. Steroid receptor coactivator-1 interacts with the p50 subunit and activates nuclear factor kappaB-mediated transactivations. J. Biol. Chem. 273:10831–10834
  • Nordeen, S. K.. 1988. Luciferase reporter gene vectors for analysis of promoters and enhancers. BioTechniques 6:454–457
  • Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., and Nakatani, Y.. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953–959
  • Oñate, S. A., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354–1357
  • Pugh, C. W., O'Rourke, J. F., Nagao, M., Gleadle, J. M., and Ratcliffe, P. J.. 1997. Activation of hypoxia-inducible factor-1; definition of regulatory domains within the α subunit. J. Biol. Chem. 272:11205–11214
  • Salceda, S., and Caro, J.. 1997. Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J. Biol. Chem. 272:22642–22647
  • Smith, C. L., Oñate, S. A., Tsai, M.-J., and O'Malley, B. W.. 1996. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc. Natl. Acad. Sci. USA 93:8884–8888
  • Sogawa, K., Nakano, R., Kobayashi, A., Kikuchi, Y., Ohe, N., Matsushita, N., and Fujii-Kuriyama, Y.. 1995. Possible function of Ah receptor nuclear translocator (Arnt) homodimer in transcriptional regulation. Proc. Natl. Acad. Sci. USA 92:1936–1940
  • Spencer, T. E., Jenster, G., Burcin, M. M., Allis, C. D., Zhou, J. X., Mizzen, C. A., McKenna, N. J., Oñate, S. A., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W.. 1997. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 389:194–198
  • Takeshita, A., Cardona, G. R., Koibuchi, N., Suen, C.-S., and Chin, W. W.. 1997. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J. Biol. Chem. 272:27629–27634
  • Torchia, J., Rose, D. W., Inostroza, J., Kamei, Y., Westin, S., Glass, C. K., and Rosenfeld, M. G.. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677–684
  • Torchia, J., Glass, C., and Rosenfeld, M. G.. 1998. Co-activators and co-repressors in the integration of the transcriptional responses. Curr. Opin. Cell Biol. 10:373–383
  • Umesono, K., Murakami, K. K., Thompson, C. C., and Evans, R. M.. 1991. Direct repeats as selective response elements for the thyroid hormone, retinoic acid and vitamin D3 receptors. Cell 65:1255–1266
  • Voegel, J. J., Heine, M. J. S., Zechel, C., Chambon, P., and Gronemeyer, H.. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667–3675
  • Voegel, J. J., Heine, M. J. S., Tini, M., Vivat, V., Chambon, P., and Gronemeyer, H.. 1998. The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17:507–519
  • Wang, G. L., Jiang, B.-H., Rue, E. A., and Semenza, G. L.. 1995. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc. Natl. Acad. Sci. USA 92:5510–5514
  • Wenger, R. H., and Gassmann, M.. 1997. Oxygen(es) and the hypoxia-inducible factor-1. Biol. Chem. 378:609–616
  • Westin, S., Kurokawa, R., Nolte, R. T., Wisely, G. B., McInerney, E. M., Rose, D. W., Milburn, M. V., Rosenfeld, M. G., and Glass, C. K.. 1998. Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators. Nature 395:199–202
  • Xanthoudakis, S., Miao, G., Wang, F., Pan, Y. C., and Curran, T.. 1992. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:3323–3335
  • Xanthoudakis, S., Miao, G. G., and Curran, T.. 1994. The redox and DNA-repair activities of Ref-1 are encoded by nonoverlapping domains. Proc. Natl. Acad. Sci. USA 91:23–27
  • Yao, K.-S., Xanthoudakis, S., Curran, T., and O'Dwyer, P. J.. 1994. Activation of AP-1 and of a nuclear redox factor, Ref-1, in the response of HT29 colon cancer cells to hypoxia. Mol. Cell. Biol. 14:5997–6003
  • Yao, T.-P., Ku, G., Zhou, N., Scully, R., and Livingston, D. M.. 1996. The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc. Natl. Acad. Sci. USA 93:10626–10631

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.