메뉴 건너뛰기




Volumn 543, Issue 7645, 2017, Pages 447-451

Hypersensitive termination of the hypoxic response by a disordered protein switch

Author keywords

[No Author keywords available]

Indexed keywords

E1A ASSOCIATED P300 PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; INTRINSICALLY DISORDERED PROTEIN; PROTEIN; PROTEIN CITED2; PROTEIN TAZ1; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; CITED2 PROTEIN, HUMAN; HIF1A PROTEIN, HUMAN; HISTONE ACETYLTRANSFERASE PCAF; OXYGEN; PROTEIN BINDING; REPRESSOR PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 85015440189     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature21705     Document Type: Article
Times cited : (130)

References (30)
  • 1
    • 84897019542 scopus 로고    scopus 로고
    • Oxygen sensing, hypoxia-inducible factors, and disease pathophysiology
    • Semenza, G. L. Oxygen sensing, hypoxia-inducible factors, and disease pathophysiology. Annu. Rev. Pathol. 9, 47-71 (2014).
    • (2014) Annu. Rev. Pathol. , vol.9 , pp. 47-71
    • Semenza, G.L.1
  • 2
    • 77956805884 scopus 로고    scopus 로고
    • Feedback regulators of hypoxia-inducible factors and their role in cancer biology
    • Henze, A.-T. & Acker, T. Feedback regulators of hypoxia-inducible factors and their role in cancer biology. Cell Cycle 9, 2821-2835 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 2821-2835
    • Henze, A.-T.1    Acker, T.2
  • 3
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang, G. L., Jiang, B. H., Rue, E. A. & Semenza, G. L. 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 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 4
    • 0029803552 scopus 로고    scopus 로고
    • An essential role for p300/CBP in the cellular response to hypoxia
    • Arany, Z. et al. An essential role for p300/CBP in the cellular response to hypoxia. Proc. Natl Acad. Sci. USA 93, 12969-12973 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12969-12973
    • Arany, Z.1
  • 6
    • 0037117479 scopus 로고    scopus 로고
    • Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1α
    • Freedman, S. J. et al. Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1α. Proc. Natl Acad. Sci. USA 99, 5367-5372 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5367-5372
    • Freedman, S.J.1
  • 7
    • 0032900610 scopus 로고    scopus 로고
    • Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1
    • Bhattacharya, S. et al. Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes Dev. 13, 64-75 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 64-75
    • Bhattacharya, S.1
  • 8
    • 1642576027 scopus 로고    scopus 로고
    • Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites
    • De Guzman, R. N., Martinez-Yamout, M. A., Dyson, H. J. & Wright, P. E. Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. J. Biol. Chem. 279, 3042-3049 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3042-3049
    • De Guzman, R.N.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 9
    • 0038392752 scopus 로고    scopus 로고
    • Structural basis for negative regulation of hypoxiainducible factor-1α by CITED2
    • Freedman, S. J. et al. Structural basis for negative regulation of hypoxiainducible factor-1α by CITED2. Nat. Struct. Biol. 10, 504-512 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 504-512
    • Freedman, S.J.1
  • 10
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright, P. E. & Dyson, H. J. Intrinsically disordered proteins in cellular signalling and regulation. Nat. Rev. Mol. Cell Biol. 16, 18-29 (2015).
    • (2015) Nat. Rev. Mol. Cell Biol. , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2
  • 11
    • 84942294146 scopus 로고    scopus 로고
    • Functional advantages of dynamic protein disorder
    • Berlow, R. B., Dyson, H. J. & Wright, P. E. Functional advantages of dynamic protein disorder. FEBS Lett. 589, 2433-2440 (2015).
    • (2015) FEBS Lett. , vol.589 , pp. 2433-2440
    • Berlow, R.B.1    Dyson, H.J.2    Wright, P.E.3
  • 12
    • 84902446852 scopus 로고    scopus 로고
    • Short linear motifs: Ubiquitous and functionally diverse protein interaction modules directing cell regulation
    • Van Roey, K. et al. Short linear motifs: ubiquitous and functionally diverse protein interaction modules directing cell regulation. Chem. Rev. 114, 6733-6778 (2014).
    • (2014) Chem. Rev. , vol.114 , pp. 6733-6778
    • Van Roey, K.1
  • 13
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-A to the von Hippel-Lindau ubiquitylation complex by O2-Regulated prolyl hydroxylation
    • Jaakkola, P. et al. Targeting of HIF-a to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292, 468-472 (2001).
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 14
    • 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. & Whitelaw, M. L. Asparagine hydroxylation of the HIF transactivation domain: a hypoxic switch. Science 295, 858-861 (2002).
    • (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
  • 15
    • 0035347260 scopus 로고    scopus 로고
    • Induction of HIF-1a in response to hypoxia is instantaneous
    • Jewell, U. R. et al. Induction of HIF-1a in response to hypoxia is instantaneous. FASEB J. 15, 1312-1314 (2001).
    • (2001) FASEB J. , vol.15 , pp. 1312-1314
    • Jewell, U.R.1
  • 16
    • 3042808208 scopus 로고    scopus 로고
    • Properties of switch-like bioregulatory networks studied by simulation of the hypoxia response control system
    • Kohn, K. W. et al. Properties of switch-like bioregulatory networks studied by simulation of the hypoxia response control system. Mol. Biol. Cell 15, 3042-3052 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3042-3052
    • Kohn, K.W.1
  • 17
    • 41149108072 scopus 로고    scopus 로고
    • CITED2 mediates the paradoxical responses of HIF-1a to proteasome inhibition
    • Shin, D. H. et al. CITED2 mediates the paradoxical responses of HIF-1a to proteasome inhibition. Oncogene 27, 1939-1944 (2008).
    • (2008) Oncogene , vol.27 , pp. 1939-1944
    • Shin, D.H.1
  • 18
    • 78650590282 scopus 로고    scopus 로고
    • Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation
    • Lee, C. W., Ferreon, J. C., Ferreon, A. C., Arai, M. & Wright, P. E. Graded enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation. Proc. Natl Acad. Sci. USA 107, 19290-19295 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19290-19295
    • Lee, C.W.1    Ferreon, J.C.2    Ferreon, A.C.3    Arai, M.4    Wright, P.E.5
  • 19
    • 11144265736 scopus 로고    scopus 로고
    • A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization
    • Roehrl, M. H. A., Wang, J. Y. & Wagner, G. A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization. Biochemistry 43, 16056-16066 (2004).
    • (2004) Biochemistry , vol.43 , pp. 16056-16066
    • Roehrl, M.H.A.1    Wang, J.Y.2    Wagner, G.3
  • 20
    • 84866720054 scopus 로고    scopus 로고
    • Interplay between allostery and intrinsic disorder in an ensemble
    • Motlagh, H. N., Li, J., Thompson, E. B. & Hilser, V. J. Interplay between allostery and intrinsic disorder in an ensemble. Biochem. Soc. Trans. 40, 975-980 (2012).
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 975-980
    • Motlagh, H.N.1    Li, J.2    Thompson, E.B.3    Hilser, V.J.4
  • 21
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon, A. C., Ferreon, J. C., Wright, P. E. & Deniz, A. A. Modulation of allostery by protein intrinsic disorder. Nature 498, 390-394 (2013).
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 22
    • 77954256912 scopus 로고    scopus 로고
    • Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity
    • Garcia-Pino, A. et al. Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell 142, 101-111 (2010).
    • (2010) Cell , vol.142 , pp. 101-111
    • Garcia-Pino, A.1
  • 23
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh, H. N., Wrabl, J. O., Li, J. & Hilser, V. J. The ensemble nature of allostery. Nature 508, 331-339 (2014).
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 24
    • 37349097703 scopus 로고    scopus 로고
    • Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes
    • Sugase, K., Landes, M. A., Wright, P. E. & Martinez-Yamout, M. Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes. Protein Expr. Purif. 57, 108-115 (2008).
    • (2008) Protein Expr. Purif. , vol.57 , pp. 108-115
    • Sugase, K.1    Landes, M.A.2    Wright, P.E.3    Martinez-Yamout, M.4
  • 26
    • 0035793584 scopus 로고    scopus 로고
    • Molecular mechanism of hypoxia-inducible factor 1a-p300 interaction. A leucine-rich interface regulated by a single cysteine
    • Gu, J., Milligan, J. & Huang, L. E. Molecular mechanism of hypoxia-inducible factor 1a-p300 interaction. A leucine-rich interface regulated by a single cysteine. J. Biol. Chem. 276, 3550-3554 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3550-3554
    • Gu, J.1    Milligan, J.2    Huang, L.E.3
  • 27
    • 84881267612 scopus 로고    scopus 로고
    • Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm
    • Anthis, N. J. & Clore, G. M. Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm. Protein Sci. 22, 851-858 (2013).
    • (2013) Protein Sci. , vol.22 , pp. 851-858
    • Anthis, N.J.1    Clore, G.M.2
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 30
    • 70149102207 scopus 로고    scopus 로고
    • Accurate sampling of high-frequency motions in proteins by steady-state 15N-{1H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation
    • Ferrage, F., Cowburn, D. & Ghose, R. Accurate sampling of high-frequency motions in proteins by steady-state 15N-{1H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation. J. Am. Chem. Soc. 131, 6048-6049 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6048-6049
    • Ferrage, F.1    Cowburn, D.2    Ghose, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.