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Volumn 116, Issue 7, 2003, Pages 1319-1326

Intracellular localisation of human HIF-1α hydroxylases: Implications for oxygen sensing

Author keywords

Hydroxylase; Hypoxia; Hypoxia inducible factor; Oxygen sensing

Indexed keywords

ASPARAGINE; HYBRID PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; LUCIFERASE; MESSENGER RNA; OXYGEN; OXYGENASE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;

EID: 0037386143     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00318     Document Type: Review
Times cited : (384)

References (42)
  • 1
    • 0035936886 scopus 로고    scopus 로고
    • HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1 alpha degradation
    • Berra, E., Richard, D. E., Gothie, E. and Pouyssegur, J. (2001). HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1 alpha degradation. FEBS Lett. 491, 85-90.
    • (2001) FEBS Lett. , vol.491 , pp. 85-90
    • Berra, E.1    Richard, D.E.2    Gothie, E.3    Pouyssegur, J.4
  • 3
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R. K. and McKnight, S. L. (2001). A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294, 1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 5
    • 0033592926 scopus 로고    scopus 로고
    • Lethal paralysis of Caenorhabditis elegans by Pseudomonas aeruginosa
    • Darby, C., Cosma, C. L., Thomas, J. H. and Manoil, C. (1999). Lethal paralysis of Caenorhabditis elegans by Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 96, 15202-15207.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15202-15207
    • Darby, C.1    Cosma, C.L.2    Thomas, J.H.3    Manoil, C.4
  • 6
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1α in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • 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 HIF1α in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 18, 1905-1914.
    • (1999) EMBO J. , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 8
    • 0036314978 scopus 로고    scopus 로고
    • Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein
    • Groulx, I. and Lee, S. (2002). Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein. Mol. Cell. Biol. 22, 5319-5336.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5319-5336
    • Groulx, I.1    Lee, S.2
  • 10
    • 0035651033 scopus 로고    scopus 로고
    • Dissecting hypoxia-dependent and hypoxia-independent steps in the HIF-1 alpha activation cascade: Implications for HIF-1alpha gene therapy
    • Hofer, T., Desbaillets, I., Hopfl, G., Gassmann, M. and Wenger, R. H. (2001). Dissecting hypoxia-dependent and hypoxia-independent steps in the HIF-1 alpha activation cascade: implications for HIF-1alpha gene therapy. FASEB J. 15, 2715-2717.
    • (2001) FASEB J. , vol.15 , pp. 2715-2717
    • Hofer, T.1    Desbaillets, I.2    Hopfl, G.3    Gassmann, M.4    Wenger, R.H.5
  • 12
    • 0037131159 scopus 로고    scopus 로고
    • Sequence determinants in hypoxia inducible factor-1α for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3
    • Huang, J., Zhao, Q., Mooney, S. M. and Lee, F. S. (2002). Sequence determinants in hypoxia inducible factor-1α for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3. J. Biol. Chem. 277, 39792-39800.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39792-39800
    • Huang, J.1    Zhao, Q.2    Mooney, S.M.3    Lee, F.S.4
  • 17
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha
    • 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-1alpha. EMBO J. 17, 6573-6586.
    • (1998) EMBO J. , vol.17 , pp. 6573-6586
    • Kallio, P.J.1    Okamoto, K.2    O'Brien, S.3    Carrero, P.4    Makino, Y.5    Tanaka, H.6    Poellinger, L.7
  • 18
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • Lando, D., Peet, D. J., Whelan, D. A., Gorman, J. J. and Whitelaw, M. L. (2002a) Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295, 858-861.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 19
    • 0037097861 scopus 로고    scopus 로고
    • FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor
    • Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L. and Bruick, R. K. (2002b). FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Genes Dev. 16, 1466-1471.
    • (2002) Genes Dev. , vol.16 , pp. 1466-1471
    • Lando, D.1    Peet, D.J.2    Gorman, J.J.3    Whelan, D.A.4    Whitelaw, M.L.5    Bruick, R.K.6
  • 20
    • 0035895928 scopus 로고    scopus 로고
    • SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons
    • Lipscomb, E. A., Sarmiere, P. D. and Freeman, R. S. (2001). SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons. J. Biol. Chem. 276, 5085-5092.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5085-5092
    • Lipscomb, E.A.1    Sarmiere, P.D.2    Freeman, R.S.3
  • 21
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: A novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon, P. C., Hirota, K. and Semenza, G. L. (2001). FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15, 2675-2686.
    • (2001) Genes Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1    Hirota, K.2    Semenza, G.L.3
  • 22
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-α chains activated by prolyl hydroxylation
    • Masson, N., Willam, C., Maxwell, P. H., Pugh, C. W. and Ratcliffe, P. J. (2001). Independent function of two destruction domains in hypoxia-inducible factor-α. chains activated by prolyl hydroxylation. EMBO J. 20, 5197-5206.
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 24
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • Min, J. H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., Jr and Pavletich, N. P. (2002). Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling. Science 296, 1886-1889.
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin W.G., Jr.5    Pavletich, N.P.6
  • 26
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein
    • Ohh, M., Park, C. W., Ivan, M., Hoffman, M. A., Kim, T. Y., Huang, L. E., Pavletich, N., Chau, V. and Kaelin, W. G. (2000). Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein. Nat. Cell Biol. 2, 423-427.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 423-427
    • Ohh, M.1    Park, C.W.2    Ivan, M.3    Hoffman, M.A.4    Kim, T.Y.5    Huang, L.E.6    Pavletich, N.7    Chau, V.8    Kaelin, W.G.9
  • 27
    • 0033593219 scopus 로고    scopus 로고
    • Oxygen-regulated and transactivating domains in endothelial PAS protein 1: Comparison with hypoxia-inducible factor-1alpha
    • O'Rourke, J. F., Tian, Y. M., Ratcliffe, P. J. and Pugh, C. W. (1999) Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1alpha. J. Biol. Chem. 274, 2060-2071.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2060-2071
    • O'Rourke, J.F.1    Tian, Y.M.2    Ratcliffe, P.J.3    Pugh, C.W.4
  • 28
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1; definition of regulatory domains within the α subunit
    • 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 30
    • 0037064141 scopus 로고    scopus 로고
    • Functional analysis of hypoxia-inducible factor-1-mediated transactivation - Identification of amino acid residues critical for transcriptional activation and/or interaction with CBP
    • Ruas, J. L., Poellinger, L. and Pereira, T. (2002). Functional analysis of hypoxia-inducible factor-1-mediated transactivation - identification of amino acid residues critical for transcriptional activation and/or interaction with CBP. J. Biol. Chem. 277, 38723-38730.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38723-38730
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 31
    • 0030961006 scopus 로고    scopus 로고
    • 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
    • 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 32
    • 0036232662 scopus 로고    scopus 로고
    • Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1α is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP
    • Sang, N., Fang, J., Srinivas, V., Leshchinsky, I. and Caro, J. (2002). Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1α is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP. Mol. Cell. Biol. 22, 2984-2992.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2984-2992
    • Sang, N.1    Fang, J.2    Srinivas, V.3    Leshchinsky, I.4    Caro, J.5
  • 34
    • 0033529656 scopus 로고    scopus 로고
    • Perspectives on oxygen sensing
    • Semenza, G. L. (1999). Perspectives on oxygen sensing. Cell 98, 281-284.
    • (1999) Cell , vol.98 , pp. 281-284
    • Semenza, G.L.1
  • 35
    • 0037165244 scopus 로고    scopus 로고
    • Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression)
    • Seth, P., Krop, I., Porter, D. and Polyak, K. (2002). Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene 21, 836-843.
    • (2002) Oncogene , vol.21 , pp. 836-843
    • Seth, P.1    Krop, I.2    Porter, D.3    Polyak, K.4
  • 36
    • 0034663894 scopus 로고    scopus 로고
    • Mechanism of regulation of the hypoxia-inducible factor-1α by the von Hippel-Lindau tumor suppressor protein
    • Tanimoto, K., Makino, Y., Pereira, T. and Poellinger, L. (2000). Mechanism of regulation of the hypoxia-inducible factor-1α. by the von Hippel-Lindau tumor suppressor protein. EMBO J. 19, 4298-4309.
    • (2000) EMBO J. , vol.19 , pp. 4298-4309
    • Tanimoto, K.1    Makino, Y.2    Pereira, T.3    Poellinger, L.4
  • 37
    • 0035812318 scopus 로고    scopus 로고
    • Characterization and comparative analysis of the EGLN gene family
    • Taylor, M. S. (2001). Characterization and comparative analysis of the EGLN gene family. Gene 275, 125-132.
    • (2001) Gene , vol.275 , pp. 125-132
    • Taylor, M.S.1
  • 38
    • 0020808726 scopus 로고
    • EGG-laying defective mutants of the nematode Caenorhabditis elegans
    • Trent, C., Tsung, N. and Horvitz, H. R. (1983). EGG-laying defective mutants of the nematode Caenorhabditis elegans. Genetics 104, 619-647.
    • (1983) Genetics , vol.104 , pp. 619-647
    • Trent, C.1    Tsung, N.2    Horvitz, H.R.3
  • 40
    • 0034107952 scopus 로고    scopus 로고
    • Mammalian oxygen sensing, signalling and gene regulation
    • Wenger, R. H. (2000). Mammalian oxygen sensing, signalling and gene regulation. J. Exp. Biol. 203, 1253-1263.
    • (2000) J. Exp. Biol. , vol.203 , pp. 1253-1263
    • Wenger, R.H.1
  • 41
    • 0036320934 scopus 로고    scopus 로고
    • 2-regulated gene expression
    • 2-regulated gene expression. FASEB J. 16, 1151-1162.
    • (2002) FASEB J. , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 42
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation
    • Yu, F., White, S. B., Zhao, Q. and Lee, F. S. (2001). HIF-1α binding to VHL is regulated by stimulus-sensitive proline hydroxylation. Proc. Natl. Acad. Sci. USA 98, 9630-9635.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Zhao, Q.3    Lee, F.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.