메뉴 건너뛰기




Volumn 346, Issue 4, 2006, Pages 1289-1296

Reconstitution of human hypoxia inducible factor HIF-1 in yeast: A simple in vivo system to identify and characterize HIF-1α effectors

Author keywords

ARNT; Cpr6; Geldanamycin; HIF 1; HIF 1 ; Hsp90; Radicicol; Sba1; Sti1; Yeast

Indexed keywords

CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; RADICICOL;

EID: 33745367639     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.06.043     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0036359548 scopus 로고    scopus 로고
    • Hypoxia-a key regulatory factor in tumour growth
    • Harris A.L. Hypoxia-a key regulatory factor in tumour growth. Nat. Rev. Cancer 2 (2002) 38-47
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 38-47
    • Harris, A.L.1
  • 2
    • 0033233243 scopus 로고    scopus 로고
    • 2 homeostasis by hypoxia-inducible factor 1
    • 2 homeostasis by hypoxia-inducible factor 1. Annu. Rev. Cell Dev. Biol. 15 (1999) 551-578
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 551-578
    • Semenza, G.L.1
  • 3
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications
    • Brahimi-Horn C., Mazure N., and Pouyssegur J. Signalling via the hypoxia-inducible factor-1α requires multiple posttranslational modifications. Cell Signal. 17 (2005) 1-9
    • (2005) Cell Signal. , vol.17 , pp. 1-9
    • Brahimi-Horn, C.1    Mazure, N.2    Pouyssegur, J.3
  • 5
    • 0036569704 scopus 로고    scopus 로고
    • Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells
    • Mabjeesh N.J., Post D.E., Willard M.T., Kaur B., Van Meir E.G., Simons J.W., and Zhong H. Geldanamycin induces degradation of hypoxia-inducible factor 1α protein via the proteosome pathway in prostate cancer cells. Cancer Res. 62 (2002) 2478-2482
    • (2002) Cancer Res. , vol.62 , pp. 2478-2482
    • Mabjeesh, N.J.1    Post, D.E.2    Willard, M.T.3    Kaur, B.4    Van Meir, E.G.5    Simons, J.W.6    Zhong, H.7
  • 6
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway
    • Isaacs J.S., Jung Y.J., Mimnaugh E.G., Martinez A., Cuttitta F., and Neckers L.M. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1α-degradative pathway. J. Biol. Chem. 277 (2002) 29936-29944
    • (2002) J. Biol. Chem. , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 9
    • 0036841843 scopus 로고    scopus 로고
    • Reduction of hypoxia-induced transcription through the repression of hypoxia-inducible factor-1α/aryl hydrocarbon receptor nuclear translocator DNA binding by the 90-kDa heat-shock protein inhibitor radicicol
    • Hur E., Kim H.H., Choi S.M., Kim J.H., Yim S., Kwon H.J., Choi Y., Kim D.K., Lee M.O., and Park H. Reduction of hypoxia-induced transcription through the repression of hypoxia-inducible factor-1α/aryl hydrocarbon receptor nuclear translocator DNA binding by the 90-kDa heat-shock protein inhibitor radicicol. Mol. Pharmacol. 62 (2002) 975-982
    • (2002) Mol. Pharmacol. , vol.62 , pp. 975-982
    • Hur, E.1    Kim, H.H.2    Choi, S.M.3    Kim, J.H.4    Yim, S.5    Kwon, H.J.6    Choi, Y.7    Kim, D.K.8    Lee, M.O.9    Park, H.10
  • 10
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G.L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3 (2003) 721-732
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 12
    • 4043119692 scopus 로고    scopus 로고
    • The HIF pathway as a therapeutic target
    • Hewitson K.S., and Schofield C.J. The HIF pathway as a therapeutic target. Drug Discov. Today 9 (2004) 704-711
    • (2004) Drug Discov. Today , vol.9 , pp. 704-711
    • Hewitson, K.S.1    Schofield, C.J.2
  • 13
    • 0032823635 scopus 로고    scopus 로고
    • Antifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug action
    • Cardenas M.E., Cruz M.C., Del Poeta M., Chung N., Perfect J.R., and Heitman J. Antifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug action. Clin. Microbiol. Rev. 12 (1999) 583-611
    • (1999) Clin. Microbiol. Rev. , vol.12 , pp. 583-611
    • Cardenas, M.E.1    Cruz, M.C.2    Del Poeta, M.3    Chung, N.4    Perfect, J.R.5    Heitman, J.6
  • 14
    • 0032766581 scopus 로고    scopus 로고
    • Investigation of steroid receptor function in the budding yeast Saccharomyces cerevisiae
    • McEwan I.J. Investigation of steroid receptor function in the budding yeast Saccharomyces cerevisiae. FEMS Microbiol. Lett. 176 (1999) 1-9
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 1-9
    • McEwan, I.J.1
  • 15
    • 0345735766 scopus 로고    scopus 로고
    • Pharmacological and genetic analysis of 90-kDa heat shock isoprotein-aryl hydrocarbon receptor complexes
    • Cox M.B., and Miller III C.A. Pharmacological and genetic analysis of 90-kDa heat shock isoprotein-aryl hydrocarbon receptor complexes. Mol. Pharmacol. 64 (2003) 1549-1556
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1549-1556
    • Cox, M.B.1    Miller III, C.A.2
  • 16
    • 0344393566 scopus 로고    scopus 로고
    • Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, co-chaperones and plasma membrane ATP binding cassette transporters of yeast
    • Piper P.W., Millson S.H., Mollapour M., Panaretou B., Siligardi G., Pearl L.H., and Prodromou C. Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, co-chaperones and plasma membrane ATP binding cassette transporters of yeast. Eur. J. Biochem. 270 (2003) 4689-4695
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4689-4695
    • Piper, P.W.1    Millson, S.H.2    Mollapour, M.3    Panaretou, B.4    Siligardi, G.5    Pearl, L.H.6    Prodromou, C.7
  • 17
    • 0032145257 scopus 로고    scopus 로고
    • Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: expression vectors with bi-directional promoters for use in Saccharomyces cerevisiae
    • Miller III C.A., Martinat M.A., and Hyman L.E. Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: expression vectors with bi-directional promoters for use in Saccharomyces cerevisiae. Nucleic Acids Res. 26 (1998) 3577-3583
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3577-3583
    • Miller III, C.A.1    Martinat, M.A.2    Hyman, L.E.3
  • 18
    • 0031438749 scopus 로고    scopus 로고
    • Expression of the human aryl hydrocarbon receptor complex in yeast. Activation of transcription by indole compounds
    • Miller III C.A. Expression of the human aryl hydrocarbon receptor complex in yeast. Activation of transcription by indole compounds. J. Biol. Chem. 272 (1997) 32824-32829
    • (1997) J. Biol. Chem. , vol.272 , pp. 32824-32829
    • Miller III, C.A.1
  • 19
    • 0029972666 scopus 로고    scopus 로고
    • Construction of a reporter plasmid that allows expression libraries to be exploited for the one-hybrid system
    • Wolf S.S., Roder K., and Schweizer M. Construction of a reporter plasmid that allows expression libraries to be exploited for the one-hybrid system. Biotechniques 20 (1996) 568-574
    • (1996) Biotechniques , vol.20 , pp. 568-574
    • Wolf, S.S.1    Roder, K.2    Schweizer, M.3
  • 20
    • 7744231036 scopus 로고    scopus 로고
    • Cobalt induces hypoxia-inducible factor-1α expression in airway smooth muscle cells by a reactive oxygen species- and PI3K-dependent mechanism
    • Chachami G., Simos G., Hatziefthimiou A., Bonanou S., Molyvdas P.A., and Paraskeva E. Cobalt induces hypoxia-inducible factor-1α expression in airway smooth muscle cells by a reactive oxygen species- and PI3K-dependent mechanism. Am. J. Respir. Cell Mol. Biol. 31 (2004) 544-551
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.31 , pp. 544-551
    • Chachami, G.1    Simos, G.2    Hatziefthimiou, A.3    Bonanou, S.4    Molyvdas, P.A.5    Paraskeva, E.6
  • 21
    • 0026468180 scopus 로고
    • A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
    • Semenza G.L., and Wang G.L. A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation. Mol. Cell. Biol. 12 (1992) 5447-5454
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 22
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D., St Jean A., Woods R.A., and Schiestl R.H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20 (1992) 1425
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 25
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
    • Fang Y., Fliss A.E., Rao J., and Caplan A.J. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18 (1998) 3727-3734
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3727-3734
    • Fang, Y.1    Fliss, A.E.2    Rao, J.3    Caplan, A.J.4
  • 26
    • 0031013723 scopus 로고    scopus 로고
    • In vivo analysis of the Hsp90 co-chaperone Sti1 (p60)
    • Chang H.C., Nathan D.F., and Lindquist S. In vivo analysis of the Hsp90 co-chaperone Sti1 (p60). Mol. Cell. Biol. 17 (1997) 318-325
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 318-325
    • Chang, H.C.1    Nathan, D.F.2    Lindquist, S.3
  • 27
    • 0029807530 scopus 로고    scopus 로고
    • A cyclophilin function in Hsp90-dependent signal transduction
    • Duina A.A., Chang H.C., Marsh J.A., Lindquist S., and Gaber R.F. A cyclophilin function in Hsp90-dependent signal transduction. Science 274 (1996) 1713-1715
    • (1996) Science , vol.274 , pp. 1713-1715
    • Duina, A.A.1    Chang, H.C.2    Marsh, J.A.3    Lindquist, S.4    Gaber, R.F.5
  • 28
    • 0037165496 scopus 로고    scopus 로고
    • The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system
    • Cox M.B., and Miller III C.A. The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system. Toxicol. Lett. 129 (2002) 13-21
    • (2002) Toxicol. Lett. , vol.129 , pp. 13-21
    • Cox, M.B.1    Miller III, C.A.2
  • 29
    • 0036229641 scopus 로고    scopus 로고
    • Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast
    • Miller C.A. Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast. Cell Signal. 14 (2002) 615-623
    • (2002) Cell Signal. , vol.14 , pp. 615-623
    • Miller, C.A.1
  • 30
    • 1842682380 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1-related diseases and prospective therapeutic tools
    • Park J.W., Chun Y.S., and Kim M.S. Hypoxia-inducible factor 1-related diseases and prospective therapeutic tools. J. Pharmacol. Sci. 94 (2004) 221-232
    • (2004) J. Pharmacol. Sci. , vol.94 , pp. 221-232
    • Park, J.W.1    Chun, Y.S.2    Kim, M.S.3
  • 33
    • 0345708353 scopus 로고    scopus 로고
    • The mammalian basic helix-loop-helix/PAS family of transcriptional regulators
    • Kewley R.J., Whitelaw M.L., and Chapman-Smith A. The mammalian basic helix-loop-helix/PAS family of transcriptional regulators. Int. J. Biochem. Cell Biol. 36 (2004) 189-204
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 189-204
    • Kewley, R.J.1    Whitelaw, M.L.2    Chapman-Smith, A.3
  • 34
    • 6044219806 scopus 로고    scopus 로고
    • Non-hypoxic transcriptional activation of the aryl hydrocarbon receptor nuclear translocator in concert with a novel hypoxia-inducible factor-1α isoform
    • Lee K.H., Park J.W., and Chun Y.S. Non-hypoxic transcriptional activation of the aryl hydrocarbon receptor nuclear translocator in concert with a novel hypoxia-inducible factor-1α isoform. Nucleic Acids Res. 32 (2004) 5499-5511
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5499-5511
    • Lee, K.H.1    Park, J.W.2    Chun, Y.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.