메뉴 건너뛰기




Volumn 408, Issue 2, 2007, Pages 231-240

Identification of a region on hypoxia-inducible-factor prolyl 4-hydroxylases that determines their specificity for the oxygen degradation domains

Author keywords

EGL nine homologue (EGLN); Hypoxia; Hypoxia inducible factor (HIF); Oxygen degradation domain (ODD); Proline hydroxylase domain (PHD); Von Hippel Lindau protein (VHL protein)

Indexed keywords

DOMAIN SWAPPING; HYPOXIA; PROLINE HYDROXYLASE DOMAINS; PROTEASOMAL DEGRADATION;

EID: 36749095315     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071052     Document Type: Article
Times cited : (32)

References (29)
  • 1
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger, R. H., Stiehl, D. P. and Camenisch, G. (2005) Integration of oxygen signaling at the consensus HRE. Sci. STKE 306, re12
    • (2005) Sci. STKE , vol.306
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 5
    • 17944375360 scopus 로고    scopus 로고
    • Epstein, A. C., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A. et al. (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54
    • Epstein, A. C., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A. et al. (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107, 43-54
  • 6
    • 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
  • 8
    • 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
  • 10
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF
    • Hirsilä, M., Koivunen, P., Günzler, V., Kivirikko, K. I. and Myllyharju, J. (2003) Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor HIF. J. Biol. Chem. 278, 30772-30780
    • (2003) J. Biol. Chem , vol.278 , pp. 30772-30780
    • Hirsilä, M.1    Koivunen, P.2    Günzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 11
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the HIF prolyl 4-hydroxylases
    • Koivunen, P., Hirsila, M., Kivirikko, K. I. and Myllyharju, J. (2006) The length of peptide substrates has a marked effect on hydroxylation by the HIF prolyl 4-hydroxylases. J. Biol. Chem. 281, 28712-28720
    • (2006) J. Biol. Chem , vol.281 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 12
    • 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
  • 13
    • 0037131159 scopus 로고    scopus 로고
    • Seguence 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) Seguence 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
  • 14
    • 11244279649 scopus 로고    scopus 로고
    • Many amino acid substitutions in a HIF-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: Substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation
    • Li, D., Hirsila, M., Koivunen, P., Brenner, M. C., Xu, L., Yang, C., Kivirikko, K. I. and Myllyharju, J. (2004) Many amino acid substitutions in a HIF-1α-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation. J. Biol. Chem. 279, 55051-55059
    • (2004) J. Biol. Chem , vol.279 , pp. 55051-55059
    • Li, D.1    Hirsila, M.2    Koivunen, P.3    Brenner, M.C.4    Xu, L.5    Yang, C.6    Kivirikko, K.I.7    Myllyharju, J.8
  • 15
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2 and PHD3 in the regulation of the hypoxia inducible factor
    • Appelhoff, R. J., Tian, Y.-M., Raval, R. R., Turley, H., Harris, A. L., Pugh, C. W., Ratcliffe, P. J. and Gleadle, J. M. (2004) Differential function of the prolyl hydroxylases PHD1, PHD2 and PHD3 in the regulation of the hypoxia inducible factor. J. Biol. Chem. 279, 38458-38465
    • (2004) J. Biol. Chem , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1    Tian, Y.-M.2    Raval, R.R.3    Turley, H.4    Harris, A.L.5    Pugh, C.W.6    Ratcliffe, P.J.7    Gleadle, J.M.8
  • 17
    • 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. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acid Res. 20, 1425
    • (1992) Nucleic Acid Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 18
    • 0035971220 scopus 로고    scopus 로고
    • Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension
    • Aragones, J., Jones, D. R., Martin, S., San Juan, M. A., Alfranca, A., Vidal, F., Vara, A., Merida, I. and Landazuri, M. O. (2001) Evidence for the involvement of diacylglycerol kinase in the activation of hypoxia-inducible transcription factor 1 by low oxygen tension. J. Biol. Chem. 276, 10548-10555
    • (2001) J. Biol. Chem , vol.276 , pp. 10548-10555
    • Aragones, J.1    Jones, D.R.2    Martin, S.3    San Juan, M.A.4    Alfranca, A.5    Vidal, F.6    Vara, A.7    Merida, I.8    Landazuri, M.O.9
  • 19
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cell by plasmid DNA
    • Chen, C. and Okayama, H. (1987) High-efficiency transformation of mammalian cell by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752
    • (1987) Mol. Cell. Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 20
    • 22544464403 scopus 로고    scopus 로고
    • Coordinate regulation of the oxygen-dependent degradation domains of hypoxia inducible factor 1α
    • Chan, D. A., Sutphin, P. D., Yen, S.-E. and Giaccia, A. J. (2005) Coordinate regulation of the oxygen-dependent degradation domains of hypoxia inducible factor 1α. Mol. Cell. Biol. 25, 6415-6426
    • (2005) Mol. Cell. Biol , vol.25 , pp. 6415-6426
    • Chan, D.A.1    Sutphin, P.D.2    Yen, S.-E.3    Giaccia, A.J.4
  • 22
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • Baker, D. and Sali, A. (2001) Protein structure prediction and structural genomics. Science 294, 93-96
    • (2001) Science , vol.294 , pp. 93-96
    • Baker, D.1    Sali, A.2
  • 23
    • 19644376763 scopus 로고    scopus 로고
    • The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)
    • Ozer, A., Wu, L. C. and Bruick, R. K. (2005) The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF). Proc. Natl. Acad. Sci. U.S.A. 102, 7481-7486
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 7481-7486
    • Ozer, A.1    Wu, L.C.2    Bruick, R.K.3
  • 24
    • 27844577728 scopus 로고    scopus 로고
    • Suppression of hypoxia-inducible factor 1α (HIF-1α) transcriptional activity by the HIF prolyl hydroxylase EGLN1
    • To, K. K. W. and Huang, L. E. (2005) Suppression of hypoxia-inducible factor 1α (HIF-1α) transcriptional activity by the HIF prolyl hydroxylase EGLN1. J. Biol. Chem. 280, 38102-38107
    • (2005) J. Biol. Chem , vol.280 , pp. 38102-38107
    • To, K.K.W.1    Huang, L.E.2
  • 25
    • 33751330425 scopus 로고    scopus 로고
    • The Caenorhabditis elegans rhy-1 gene inhibits HIF-1 hypoxia-inducible factor activity in a negative feedback loop that does not include vhl-1
    • Shen, C., Shao, Z. and Powell-Coffman, J. A. (2006) The Caenorhabditis elegans rhy-1 gene inhibits HIF-1 hypoxia-inducible factor activity in a negative feedback loop that does not include vhl-1. Genetics 174, 1205-1214
    • (2006) Genetics , vol.174 , pp. 1205-1214
    • Shen, C.1    Shao, Z.2    Powell-Coffman, J.A.3
  • 26
    • 27844605466 scopus 로고    scopus 로고
    • Inhibition of the catalytic activity of hypoxia-inducible factor-1α prolyl-hydroxylase 2 by a MYND-type zinc finger
    • Choi, K.-O., Lee, T., Lee, N., Kim, J.-H., Yang, E. G., Yoon, J. M., Kim, J. H., Lee, T. G. and Park, H. (2005) Inhibition of the catalytic activity of hypoxia-inducible factor-1α prolyl-hydroxylase 2 by a MYND-type zinc finger. Mol. Pharmacol. 68, 1803-1809
    • (2005) Mol. Pharmacol , vol.68 , pp. 1803-1809
    • Choi, K.-O.1    Lee, T.2    Lee, N.3    Kim, J.-H.4    Yang, E.G.5    Yoon, J.M.6    Kim, J.H.7    Lee, T.G.8    Park, H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.