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Volumn 291, Issue 5, 2016, Pages 2196-2222

High affinity heme binding to a heme regulatory motif on the nuclear receptor rev-erbβ leads to its degradation and indirectly regulates its interaction with nuclear receptor corepressor

Author keywords

[No Author keywords available]

Indexed keywords

BINS; GENE EXPRESSION; GENES; LIGANDS; PEPTIDES; PROTEINS; RATE CONSTANTS; TRANSCRIPTION;

EID: 84956999697     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.670281     Document Type: Article
Times cited : (44)

References (110)
  • 1
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda, A., and Pascual, A. (2001) Nuclear hormone receptors and gene expression. Physiol. Rev. 81, 1269-1304
    • (2001) Physiol. Rev. , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 2
    • 0024522826 scopus 로고
    • Anovel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbAα transcriptional unit
    • Lazar, M. A., Hodin, R. A., Darling, D. S., and Chin, W. W. (1989)Anovel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbAα transcriptional unit. Mol. Cell. Biol. 9, 1128-1136
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1128-1136
    • Lazar, M.A.1    Hodin, R.A.2    Darling, D.S.3    Chin, W.W.4
  • 4
    • 0028097504 scopus 로고
    • Identification of a novel member of the nuclear receptor superfamily which is closely related to Rev-ErbA
    • Enmark, E., Kainu, T., Pelto-Huikko, M., and Gustafsson, J. A. (1994) Identification of a novel member of the nuclear receptor superfamily which is closely related to Rev-ErbA. Biochem. Biophys. Res. Commun. 204, 49-56
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 49-56
    • Enmark, E.1    Kainu, T.2    Pelto-Huikko, M.3    Gustafsson, J.A.4
  • 5
    • 0343707855 scopus 로고    scopus 로고
    • Molecular cloning and brain localization of HZF-2α, a new member of the Rev-erb subfamily of orphan nuclear receptors
    • Peña-de-Ortiz, S., and Jamieson, G. A., Jr. (1997) Molecular cloning and brain localization of HZF-2α, a new member of the Rev-erb subfamily of orphan nuclear receptors. J. Neurobiol. 32, 341-358
    • (1997) J. Neurobiol. , vol.32 , pp. 341-358
    • Peña-De-Ortiz, S.1    Jamieson, G.A.2
  • 6
    • 84859329911 scopus 로고    scopus 로고
    • Rev-erbα and Rev-erbβ coordinately protect the circadian clock and normal metabolic function
    • Bugge, A., Feng, D., Everett, L. J., Briggs, E. R., Mullican, S. E., Wang, F., Jager, J., and Lazar, M. A. (2012) Rev-erbα and Rev-erbβ coordinately protect the circadian clock and normal metabolic function. Genes Dev. 26, 657-667
    • (2012) Genes Dev. , vol.26 , pp. 657-667
    • Bugge, A.1    Feng, D.2    Everett, L.J.3    Briggs, E.R.4    Mullican, S.E.5    Wang, F.6    Jager, J.7    Lazar, M.A.8
  • 8
    • 0027998666 scopus 로고
    • Identification of RVR, a novel orphan nuclear receptor that acts as a negative transcriptional regulator
    • Retnakaran, R., Flock, G., and Giguère, V. (1994) Identification of RVR, a novel orphan nuclear receptor that acts as a negative transcriptional regulator. Mol. Endocrinol. 8, 1234-1244
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1234-1244
    • Retnakaran, R.1    Flock, G.2    Giguère, V.3
  • 9
    • 0027946824 scopus 로고
    • Rev-erbβ, a new member of the nuclear receptor superfamily, is expressed in the nervous system during chicken development
    • Bonnelye, E., Vanacker, J. M., Desbiens, X., Begue, A., Stehelin, D., and Laudet, V. (1994) Rev-erbβ, a new member of the nuclear receptor superfamily, is expressed in the nervous system during chicken development. Cell Growth Differ. 5, 1357-1365
    • (1994) Cell Growth Differ. , vol.5 , pp. 1357-1365
    • Bonnelye, E.1    Vanacker, J.M.2    Desbiens, X.3    Begue, A.4    Stehelin, D.5    Laudet, V.6
  • 12
    • 0032511229 scopus 로고    scopus 로고
    • A serum shock induces circadian gene expression in mammalian tissue culture cells
    • Balsalobre, A., Damiola, F., and Schibler, U. (1998) A serum shock induces circadian gene expression in mammalian tissue culture cells. Cell 93, 929-937
    • (1998) Cell , vol.93 , pp. 929-937
    • Balsalobre, A.1    Damiola, F.2    Schibler, U.3
  • 13
    • 0037178787 scopus 로고    scopus 로고
    • The orphan nuclear receptor REVERB α controls circadian transcription within the positive limb of the mammalian circadian oscillator
    • Preitner, N., Damiola, F., Lopez-Molina, L., Zakany, J., Duboule, D., Albrecht, U., and Schibler, U. (2002) The orphan nuclear receptor REVERB α controls circadian transcription within the positive limb of the mammalian circadian oscillator. Cell 110, 251-260
    • (2002) Cell , vol.110 , pp. 251-260
    • Preitner, N.1    Damiola, F.2    Lopez-Molina, L.3    Zakany, J.4    Duboule, D.5    Albrecht, U.6    Schibler, U.7
  • 14
    • 79953178583 scopus 로고    scopus 로고
    • Direct regulation of CLOCK expression by REV-ERB
    • Crumbley, C., and Burris, T. P. (2011) Direct regulation of CLOCK expression by REV-ERB. PLoS One 6, e17290
    • (2011) PLoS One , vol.6
    • Crumbley, C.1    Burris, T.P.2
  • 15
    • 0029962860 scopus 로고    scopus 로고
    • A functional Rev-erbα responsive element located in the human Rev-erbα promoter mediates a repressing activity
    • Adelmant, G., Bègue, A., Stéhelin, D., and Laudet, V. (1996) A functional Rev-erbα responsive element located in the human Rev-erbα promoter mediates a repressing activity. Proc. Natl. Acad. Sci. U.S.A. 93, 3553-3558
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3553-3558
    • Adelmant, G.1    Bègue, A.2    Stéhelin, D.3    Laudet, V.4
  • 18
    • 0037178861 scopus 로고    scopus 로고
    • Orphan nuclear hormone receptor Rev-erbα regulates the human apolipoprotein CIII promoter
    • Coste, H., and Rodríguez, J. C. (2002) Orphan nuclear hormone receptor Rev-erbα regulates the human apolipoprotein CIII promoter. J. Biol. Chem. 277, 27120-27129
    • (2002) J. Biol. Chem. , vol.277 , pp. 27120-27129
    • Coste, H.1    Rodríguez, J.C.2
  • 19
    • 15744394575 scopus 로고    scopus 로고
    • Reverbβ regulates the expression of genes involved in lipid absorption in skeletal muscle cells: Evidence for cross-talk between orphan nuclear receptors and myokines
    • Ramakrishnan, S. N., Lau, P., Burke, L. J., and Muscat, G. E. (2005) Reverbβ regulates the expression of genes involved in lipid absorption in skeletal muscle cells: evidence for cross-talk between orphan nuclear receptors and myokines. J. Biol. Chem. 280, 8651-8659
    • (2005) J. Biol. Chem. , vol.280 , pp. 8651-8659
    • Ramakrishnan, S.N.1    Lau, P.2    Burke, L.J.3    Muscat, G.E.4
  • 21
  • 22
    • 84897111311 scopus 로고    scopus 로고
    • Modulation of nuclear receptor function by cellular redox poise
    • Carter, E. L., and Ragsdale, S. W. (2014) Modulation of nuclear receptor function by cellular redox poise. J. Inorg. Biochem. 133, 92-103
    • (2014) J. Inorg. Biochem. , vol.133 , pp. 92-103
    • Carter, E.L.1    Ragsdale, S.W.2
  • 23
    • 78649324289 scopus 로고    scopus 로고
    • Structural and functional insights into nuclear receptor signaling
    • Jin, L., and Li, Y. (2010) Structural and functional insights into nuclear receptor signaling. Adv. Drug Deliv. Rev. 62, 1218-1226
    • (2010) Adv. Drug Deliv. Rev. , vol.62 , pp. 1218-1226
    • Jin, L.1    Li, Y.2
  • 24
    • 0034975063 scopus 로고    scopus 로고
    • The specificity of interactions between nuclear hormone receptors and corepressors is mediated by distinct amino acid sequences within the interacting domains
    • Cohen, R. N., Brzostek, S., Kim, B., Chorev, M., Wondisford, F. E., and Hollenberg, A. N. (2001) The specificity of interactions between nuclear hormone receptors and corepressors is mediated by distinct amino acid sequences within the interacting domains. Mol. Endocrinol. 15, 1049-1061
    • (2001) Mol. Endocrinol. , vol.15 , pp. 1049-1061
    • Cohen, R.N.1    Brzostek, S.2    Kim, B.3    Chorev, M.4    Wondisford, F.E.5    Hollenberg, A.N.6
  • 26
    • 84876912279 scopus 로고    scopus 로고
    • Emerging roles of the corepressors NCoR1 and SMRT in homeostasis
    • Mottis, A., Mouchiroud, L., and Auwerx, J. (2013) Emerging roles of the corepressors NCoR1 and SMRT in homeostasis. Genes Dev. 27, 819-835
    • (2013) Genes Dev. , vol.27 , pp. 819-835
    • Mottis, A.1    Mouchiroud, L.2    Auwerx, J.3
  • 28
    • 82655181792 scopus 로고    scopus 로고
    • Nuclear hormone receptor co-repressors: Structure and function
    • Watson, P. J., Fairall, L., and Schwabe, J. W. (2012) Nuclear hormone receptor co-repressors: structure and function. Mol. Cell. Endocrinol. 348, 440-449
    • (2012) Mol. Cell. Endocrinol. , vol.348 , pp. 440-449
    • Watson, P.J.1    Fairall, L.2    Schwabe, J.W.3
  • 29
    • 34748836883 scopus 로고    scopus 로고
    • Structural insight into the constitutive repression function of the nuclear receptor Rev-erbβ
    • Woo, E. J., Jeong, D. G., Lim, M. Y., Kim, S. J., Kim, K. J., Yoon, S. M., Park, B. C., and Ryu, S. E. (2007) Structural insight into the constitutive repression function of the nuclear receptor Rev-erbβ. J. Mol. Biol. 373, 735-744
    • (2007) J. Mol. Biol. , vol.373 , pp. 735-744
    • Woo, E.J.1    Jeong, D.G.2    Lim, M.Y.3    Kim, S.J.4    Kim, K.J.5    Yoon, S.M.6    Park, B.C.7    Ryu, S.E.8
  • 31
    • 0024511936 scopus 로고
    • Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus
    • Miyajima, N., Horiuchi, R., Shibuya, Y., Fukushige, S., Matsubara, K., Toyoshima, K., and Yamamoto, T. (1989) Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus. Cell 57, 31-39
    • (1989) Cell , vol.57 , pp. 31-39
    • Miyajima, N.1    Horiuchi, R.2    Shibuya, Y.3    Fukushige, S.4    Matsubara, K.5    Toyoshima, K.6    Yamamoto, T.7
  • 32
    • 0024241354 scopus 로고
    • Identification of two novel members of erbA superfamily by molecular cloning: The gene products of the two are highly related to each other
    • Miyajima, N., Kadowaki, Y., Fukushige, S., Shimizu, S., Semba, K., Yamanashi, Y., Matsubara, K., Toyoshima, K., and Yamamoto, T. (1988) Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other. Nucleic Acids Res. 16, 11057-11074
    • (1988) Nucleic Acids Res. , vol.16 , pp. 11057-11074
    • Miyajima, N.1    Kadowaki, Y.2    Fukushige, S.3    Shimizu, S.4    Semba, K.5    Yamanashi, Y.6    Matsubara, K.7    Toyoshima, K.8    Yamamoto, T.9
  • 35
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L., and Guarente, L. (1995) Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J. 14, 313-320
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 38
    • 79953012491 scopus 로고    scopus 로고
    • Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor Rev-erbβ
    • Gupta, N., and Ragsdale, S. W. (2011) Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor Rev-erbβ. J. Biol. Chem. 286, 4392-4403
    • (2011) J. Biol. Chem. , vol.286 , pp. 4392-4403
    • Gupta, N.1    Ragsdale, S.W.2
  • 39
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Qi, Z., Hamza, I., and O'Brian, M. R. (1999) Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein. Proc. Natl. Acad. Sci. U.S.A. 96, 13056-13061
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 40
    • 49649105752 scopus 로고    scopus 로고
    • Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2α kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins
    • Igarashi, J., Murase, M., Iizuka, A., Pichierri, F., Martinkova, M., and Shimizu, T. (2008) Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2α kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins. J. Biol. Chem. 283, 18782-18791
    • (2008) J. Biol. Chem. , vol.283 , pp. 18782-18791
    • Igarashi, J.1    Murase, M.2    Iizuka, A.3    Pichierri, F.4    Martinkova, M.5    Shimizu, T.6
  • 42
    • 4644371570 scopus 로고    scopus 로고
    • Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase
    • Munakata, H., Sun, J. Y., Yoshida, K., Nakatani, T., Honda, E., Hayakawa, S., Furuyama, K., and Hayashi, N. (2004) Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase. J. Biochem. 136, 233-238
    • (2004) J. Biochem. , vol.136 , pp. 233-238
    • Munakata, H.1    Sun, J.Y.2    Yoshida, K.3    Nakatani, T.4    Honda, E.5    Hayakawa, S.6    Furuyama, K.7    Hayashi, N.8
  • 43
    • 0033873749 scopus 로고    scopus 로고
    • Functional analysis of heme regulatory elements of the transcriptional activator Hap1
    • Hon, T., Hach, A., Lee, H. C., Cheng, T., and Zhang, L. (2000) Functional analysis of heme regulatory elements of the transcriptional activator Hap1. Biochem. Biophys. Res. Commun. 273, 584-591
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 584-591
    • Hon, T.1    Hach, A.2    Lee, H.C.3    Cheng, T.4    Zhang, L.5
  • 44
    • 22544452148 scopus 로고    scopus 로고
    • Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2
    • Ishikawa, H., Kato, M., Hori, H., Ishimori, K., Kirisako, T., Tokunaga, F., and Iwai, K. (2005) Involvement of heme regulatory motif in heme-mediated ubiquitination and degradation of IRP2. Mol. Cell 19, 171-181
    • (2005) Mol. Cell , vol.19 , pp. 171-181
    • Ishikawa, H.1    Kato, M.2    Hori, H.3    Ishimori, K.4    Kirisako, T.5    Tokunaga, F.6    Iwai, K.7
  • 46
    • 84928944221 scopus 로고    scopus 로고
    • Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme
    • Bagai, I., Sarangi, R., Fleischhacker, A. S., Sharma, A., Hoffman, B. M., Zuiderweg, E. R., and Ragsdale, S. W. (2015) Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme. Biochemistry 54, 2693-2708
    • (2015) Biochemistry , vol.54 , pp. 2693-2708
    • Bagai, I.1    Sarangi, R.2    Fleischhacker, A.S.3    Sharma, A.4    Hoffman, B.M.5    Zuiderweg, E.R.6    Ragsdale, S.W.7
  • 47
    • 79960401027 scopus 로고    scopus 로고
    • Nitric oxide coordinates metabolism, growth, and development via the nuclear receptor E75
    • Cáceres, L., Necakov, A. S., Schwartz, C., Kimber, S., Roberts, I. J., and Krause, H. M. (2011) Nitric oxide coordinates metabolism, growth, and development via the nuclear receptor E75. Genes Dev. 25, 1476-1485
    • (2011) Genes Dev. , vol.25 , pp. 1476-1485
    • Cáceres, L.1    Necakov, A.S.2    Schwartz, C.3    Kimber, S.4    Roberts, I.J.5    Krause, H.M.6
  • 49
    • 84857383238 scopus 로고    scopus 로고
    • Characterization of heme ligation properties of Rv0203, a secreted heme-binding protein involved in Mycobacterium tuberculosis heme uptake
    • Owens, C. P., Du, J., Dawson, J. H., and Goulding, C. W. (2012) Characterization of heme ligation properties of Rv0203, a secreted heme-binding protein involved in Mycobacterium tuberculosis heme uptake. Biochemistry 51, 1518-1531
    • (2012) Biochemistry , vol.51 , pp. 1518-1531
    • Owens, C.P.1    Du, J.2    Dawson, J.H.3    Goulding, C.W.4
  • 50
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols, L., Gu, M., Dieckman, L., Raffen, R., Collart, F. R., and Donnelly, M. I. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr. Purif. 25, 8-15
    • (2002) Protein Expr. Purif. , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 51
    • 77649176543 scopus 로고    scopus 로고
    • Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies
    • Zhou, P., and Wagner, G. (2010) Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies. J. Biomol. NMR 46, 23-31
    • (2010) J. Biomol. NMR , vol.46 , pp. 23-31
    • Zhou, P.1    Wagner, G.2
  • 53
    • 84908428449 scopus 로고    scopus 로고
    • Protein/protein interactions in the mammalian heme degradation pathway: Heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase
    • Spencer, A. L., Bagai, I., Becker, D. F., Zuiderweg, E. R., and Ragsdale, S. W. (2014) Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase. J. Biol. Chem. 289, 29836-29858
    • (2014) J. Biol. Chem. , vol.289 , pp. 29836-29858
    • Spencer, A.L.1    Bagai, I.2    Becker, D.F.3    Zuiderweg, E.R.4    Ragsdale, S.W.5
  • 54
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 55
    • 0036415329 scopus 로고    scopus 로고
    • Removal of DnaK contamination during fusion protein purifications
    • Rial, D. V., and Ceccarelli, E. A. (2002) Removal of DnaK contamination during fusion protein purifications. Protein Expr. Purif. 25, 503-507
    • (2002) Protein Expr. Purif. , vol.25 , pp. 503-507
    • Rial, D.V.1    Ceccarelli, E.A.2
  • 57
    • 4243597592 scopus 로고    scopus 로고
    • Protein-ligand binding equilibria
    • John Wiley & Sons, Inc., New York
    • Copeland, R. A. (2002) Protein-ligand binding equilibria, in Enzymes, pp 76-108, John Wiley & Sons, Inc., New York
    • (2002) Enzymes , pp. 76-108
    • Copeland, R.A.1
  • 58
    • 34548159927 scopus 로고    scopus 로고
    • Interaction of heme and heme-hemopexin with an extracellular oxidant system used to measure cell growth-associated plasma membrane electron transport
    • Rish, K. R., Swartzlander, R., Sadikot, T. N., Berridge, M. V., and Smith, A. (2007) Interaction of heme and heme-hemopexin with an extracellular oxidant system used to measure cell growth-associated plasma membrane electron transport. Biochim. Biophys. Acta 1767, 1107-1117
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1107-1117
    • Rish, K.R.1    Swartzlander, R.2    Sadikot, T.N.3    Berridge, M.V.4    Smith, A.5
  • 63
    • 0347993077 scopus 로고    scopus 로고
    • Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis
    • Mitkova, A. V., Khopde, S. M., and Biswas, S. B. (2003) Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J. Biol. Chem. 278, 52253-52261
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 64
    • 38949201270 scopus 로고    scopus 로고
    • Application of an environmentally sensitive fluorophore for rapid analysis of the binding and internalization efficiency of gene carriers
    • Bergen, J. M., Kwon, E. J., Shen, T. W., and Pun, S. H. (2008) Application of an environmentally sensitive fluorophore for rapid analysis of the binding and internalization efficiency of gene carriers. Bioconjug. Chem. 19, 377-384
    • (2008) Bioconjug. Chem. , vol.19 , pp. 377-384
    • Bergen, J.M.1    Kwon, E.J.2    Shen, T.W.3    Pun, S.H.4
  • 65
    • 0025879299 scopus 로고
    • Characterization of an unusual thyroid response unit in the promoter of the human placental lactogen gene
    • Voz, M. L., Peers, B., Belayew, A., and Martial, J. A. (1991) Characterization of an unusual thyroid response unit in the promoter of the human placental lactogen gene. J. Biol. Chem. 266, 13397-13404
    • (1991) J. Biol. Chem. , vol.266 , pp. 13397-13404
    • Voz, M.L.1    Peers, B.2    Belayew, A.3    Martial, J.A.4
  • 66
    • 0035830908 scopus 로고    scopus 로고
    • Thyroid hormone response element sequence and the recruitment of retinoid X receptors for thyroid hormone responsiveness
    • Wu, Y., Xu, B., and Koenig, R. J. (2001) Thyroid hormone response element sequence and the recruitment of retinoid X receptors for thyroid hormone responsiveness. J. Biol. Chem. 276, 3929-3936
    • (2001) J. Biol. Chem. , vol.276 , pp. 3929-3936
    • Wu, Y.1    Xu, B.2    Koenig, R.J.3
  • 67
    • 0001452326 scopus 로고
    • Fluorometric microdetermination of heme protein
    • Morrison, G. R. (1965) Fluorometric microdetermination of heme protein. Anal. Chem. 37, 1124-1126
    • (1965) Anal. Chem. , vol.37 , pp. 1124-1126
    • Morrison, G.R.1
  • 68
    • 0017184389 scopus 로고
    • Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976)Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 69
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 70
    • 84886948594 scopus 로고    scopus 로고
    • The TGFβ1 pathway is required for NFκB-dependent gene expression in mouse keratinocytes
    • Hogan, K. A., Ravindran, A., Podolsky, M. A., and Glick, A. B. (2013) The TGFβ1 pathway is required for NFκB-dependent gene expression in mouse keratinocytes. Cytokine 64, 652-659
    • (2013) Cytokine , vol.64 , pp. 652-659
    • Hogan, K.A.1    Ravindran, A.2    Podolsky, M.A.3    Glick, A.B.4
  • 72
    • 0037168586 scopus 로고    scopus 로고
    • Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
    • Mammalian Gene Collection Program Team (2002) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. U.S.A. 99, 16899-16903
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16899-16903
  • 73
    • 67749119974 scopus 로고    scopus 로고
    • Nuclear receptors Homo sapiens Rev-erbβ and Drosophila melanogaster E75 are thiolate-ligated heme proteins which undergo redox-mediated ligand switching and bind CO and NO
    • Marvin, K. A., Reinking, J. L., Lee, A. J., Pardee, K., Krause, H. M., and Burstyn, J. N. (2009) Nuclear receptors Homo sapiens Rev-erbβ and Drosophila melanogaster E75 are thiolate-ligated heme proteins which undergo redox-mediated ligand switching and bind CO and NO. Biochemistry 48, 7056-7071
    • (2009) Biochemistry , vol.48 , pp. 7056-7071
    • Marvin, K.A.1    Reinking, J.L.2    Lee, A.J.3    Pardee, K.4    Krause, H.M.5    Burstyn, J.N.6
  • 74
    • 0034730064 scopus 로고    scopus 로고
    • Characterization of the heme in human cystathionine β-synthase by Xray absorption and electron paramagnetic resonance spectroscopies
    • Ojha, S., Hwang, J., Kabil, O., Penner-Hahn, J. E., and Banerjee, R. (2000) Characterization of the heme in human cystathionine β-synthase by Xray absorption and electron paramagnetic resonance spectroscopies. Biochemistry 39, 10542-10547
    • (2000) Biochemistry , vol.39 , pp. 10542-10547
    • Ojha, S.1    Hwang, J.2    Kabil, O.3    Penner-Hahn, J.E.4    Banerjee, R.5
  • 75
    • 33747513241 scopus 로고    scopus 로고
    • Characterization of heme-regulated eIF2α kinase: Roles of the N-terminal domain in the oligomeric state, heme binding, catalysis, and inhibition
    • Miksanova, M., Igarashi, J., Minami, M., Sagami, I., Yamauchi, S., Kurokawa, H., and Shimizu, T. (2006) Characterization of heme-regulated eIF2α kinase: Roles of the N-terminal domain in the oligomeric state, heme binding, catalysis, and inhibition. Biochemistry 45, 9894-9905
    • (2006) Biochemistry , vol.45 , pp. 9894-9905
    • Miksanova, M.1    Igarashi, J.2    Minami, M.3    Sagami, I.4    Yamauchi, S.5    Kurokawa, H.6    Shimizu, T.7
  • 76
    • 0021528407 scopus 로고
    • Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme
    • Omura, T., Sadano, H., Hasegawa, T., Yoshida, Y., and Kominami, S. (1984) Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme. J. Biochem. (Tokyo) 96, 1491-1500
    • (1984) J. Biochem. (Tokyo) , vol.96 , pp. 1491-1500
    • Omura, T.1    Sadano, H.2    Hasegawa, T.3    Yoshida, Y.4    Kominami, S.5
  • 77
    • 1942469554 scopus 로고    scopus 로고
    • Activation of heme-regulated eukaryotic initi-ation factor 2α kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: Optical absorption, electron spin resonance, and resonance Raman spectral studies
    • Igarashi, J., Sato, A., Kitagawa, T., Yoshimura, T., Yamauchi, S., Sagami, I., and Shimizu, T. (2004) Activation of heme-regulated eukaryotic initi-ation factor 2α kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: Optical absorption, electron spin resonance, and resonance Raman spectral studies. J. Biol. Chem. 279, 15752-15762
    • (2004) J. Biol. Chem. , vol.279 , pp. 15752-15762
    • Igarashi, J.1    Sato, A.2    Kitagawa, T.3    Yoshimura, T.4    Yamauchi, S.5    Sagami, I.6    Shimizu, T.7
  • 78
    • 0023932566 scopus 로고
    • Detection of hemin release during hemoglobin S denaturation
    • Liu, S. C., Zhai, S., and Palek, J. (1988) Detection of hemin release during hemoglobin S denaturation. Blood 71, 1755-1758
    • (1988) Blood , vol.71 , pp. 1755-1758
    • Liu, S.C.1    Zhai, S.2    Palek, J.3
  • 79
  • 81
    • 0029150186 scopus 로고
    • The monomer-binding orphan receptor Rev-Erb represses transcription as a dimer on a novel direct repeat
    • Harding, H. P., and Lazar, M. A. (1995) The monomer-binding orphan receptor Rev-Erb represses transcription as a dimer on a novel direct repeat. Mol. Cell. Biol. 15, 4791-4802
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4791-4802
    • Harding, H.P.1    Lazar, M.A.2
  • 82
    • 0030294743 scopus 로고    scopus 로고
    • Expression, purification, and functional analysis of the DNA binding domain of the nuclear receptor Rev-Erbβ
    • Terenzi, H., Cassia, R. O., and Zakin, M. M. (1996) Expression, purification, and functional analysis of the DNA binding domain of the nuclear receptor Rev-Erbβ. Protein Expr. Purif. 8, 313-318
    • (1996) Protein Expr. Purif. , vol.8 , pp. 313-318
    • Terenzi, H.1    Cassia, R.O.2    Zakin, M.M.3
  • 83
    • 77949317555 scopus 로고    scopus 로고
    • Molecular determinants required for selective interactions between the thyroid hormone receptor homodimer and the nuclear receptor corepressor N-CoR
    • Kim, J. Y., Son, Y. L., Kim, J. S., and Lee, Y. C. (2010) Molecular determinants required for selective interactions between the thyroid hormone receptor homodimer and the nuclear receptor corepressor N-CoR. J. Mol. Biol. 396, 747-760
    • (2010) J. Mol. Biol. , vol.396 , pp. 747-760
    • Kim, J.Y.1    Son, Y.L.2    Kim, J.S.3    Lee, Y.C.4
  • 84
    • 0032230251 scopus 로고    scopus 로고
    • Two separate NCoR (nuclear receptor corepressor) interaction domains mediate corepressor action on thyroid hormone response elements
    • Cohen, R. N., Wondisford, F. E., and Hollenberg, A. N. (1998) Two separate NCoR (nuclear receptor corepressor) interaction domains mediate corepressor action on thyroid hormone response elements. Mol. Endocrinol. 12, 1567-1581
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1567-1581
    • Cohen, R.N.1    Wondisford, F.E.2    Hollenberg, A.N.3
  • 85
    • 41149132147 scopus 로고    scopus 로고
    • Bifunctional role of Rev-erbα in adipocyte differentiation
    • Wang, J., and Lazar, M. A. (2008) Bifunctional role of Rev-erbα in adipocyte differentiation. Mol. Cell. Biol. 28, 2213-2220
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2213-2220
    • Wang, J.1    Lazar, M.A.2
  • 88
    • 77954990538 scopus 로고    scopus 로고
    • Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element
    • Chen, Y., and Young, M. A. (2010) Structure of a thyroid hormone receptor DNA-binding domain homodimer bound to an inverted palindrome DNA response element. Mol. Endocrinol. 24, 1650-1664
    • (2010) Mol. Endocrinol. , vol.24 , pp. 1650-1664
    • Chen, Y.1    Young, M.A.2
  • 89
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • Hargrove, M. S., Barrick, D., and Olson, J. S. (1996) The association rate constant for heme binding to globin is independent of protein structure. Biochemistry 35, 11293-11299
    • (1996) Biochemistry , vol.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 90
    • 33144465537 scopus 로고    scopus 로고
    • Nuclear receptor Rev-erbα is a critical lithium-sensitive component of the circadian clock
    • Yin, L., Wang, J., Klein, P. S., and Lazar, M. A. (2006) Nuclear receptor Rev-erbα is a critical lithium-sensitive component of the circadian clock. Science 311, 1002-1005
    • (2006) Science , vol.311 , pp. 1002-1005
    • Yin, L.1    Wang, J.2    Klein, P.S.3    Lazar, M.A.4
  • 91
    • 38349059257 scopus 로고    scopus 로고
    • The orphan nuclear receptor Rev-erbβ recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter
    • Wang, J., Liu, N., Liu, Z., Li, Y., Song, C., Yuan, H., Li, Y. Y., Zhao, X., and Lu, H. (2008) The orphan nuclear receptor Rev-erbβ recruits Tip60 and HDAC1 to regulate apolipoprotein CIII promoter. Biochim. Biophys. Acta 1783, 224-236
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 224-236
    • Wang, J.1    Liu, N.2    Liu, Z.3    Li, Y.4    Song, C.5    Yuan, H.6    Li, Y.Y.7    Zhao, X.8    Lu, H.9
  • 92
    • 34848903026 scopus 로고    scopus 로고
    • A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbβ and removes Rev-erbβ-induced inhibition of apoCIII transcription
    • Wang, J., Li, Y., Zhang, M., Liu, Z., Wu, C., Yuan, H., Li, Y. Y., Zhao, X., and Lu, H. (2007) A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with orphan nuclear hormone receptor Rev-erbβ and removes Rev-erbβ-induced inhibition of apoCIII transcription. FEBS J. 274, 5370-5381
    • (2007) FEBS J. , vol.274 , pp. 5370-5381
    • Wang, J.1    Li, Y.2    Zhang, M.3    Liu, Z.4    Wu, C.5    Yuan, H.6    Li, Y.Y.7    Zhao, X.8    Lu, H.9
  • 93
    • 0141621135 scopus 로고    scopus 로고
    • The orphan nuclear receptor Rev-Erbα is a peroxisome proliferator-activated receptor (PPAR) γ target gene and promotes PPARγ-induced adipocyte differentiation
    • Fontaine, C., Dubois, G., Duguay, Y., Helledie, T., Vu-Dac, N., Gervois, P., Soncin, F., Mandrup, S., Fruchart, J. C., Fruchart-Najib, J., and Staels, B. (2003) The orphan nuclear receptor Rev-Erbα is a peroxisome proliferator-activated receptor (PPAR) γ target gene and promotes PPARγ-induced adipocyte differentiation. J. Biol. Chem. 278, 37672-37680
    • (2003) J. Biol. Chem. , vol.278 , pp. 37672-37680
    • Fontaine, C.1    Dubois, G.2    Duguay, Y.3    Helledie, T.4    Vu-Dac, N.5    Gervois, P.6    Soncin, F.7    Mandrup, S.8    Fruchart, J.C.9    Fruchart-Najib, J.10    Staels, B.11
  • 94
    • 77954911030 scopus 로고    scopus 로고
    • E3 ligases Arf-bp1 and Pam mediate lithium-stimulated degradation of the circadian heme receptor Rev-erbα
    • Yin, L., Joshi, S., Wu, N., Tong, X., and Lazar, M. A. (2010) E3 ligases Arf-bp1 and Pam mediate lithium-stimulated degradation of the circadian heme receptor Rev-erbα. Proc. Natl. Acad. Sci. U.S.A. 107, 11614-11619
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11614-11619
    • Yin, L.1    Joshi, S.2    Wu, N.3    Tong, X.4    Lazar, M.A.5
  • 96
    • 0037194790 scopus 로고    scopus 로고
    • Coordination of circadian timing in mammals
    • Reppert, S. M., and Weaver, D. R. (2002) Coordination of circadian timing in mammals. Nature 418, 935-941
    • (2002) Nature , vol.418 , pp. 935-941
    • Reppert, S.M.1    Weaver, D.R.2
  • 98
    • 70349734885 scopus 로고    scopus 로고
    • Heme reversibly damps PERIOD2 rhythms in mouse suprachiasmatic nucleus explants
    • Guenthner, C. J., Bickar, D., and Harrington, M. E. (2009) Heme reversibly damps PERIOD2 rhythms in mouse suprachiasmatic nucleus explants. Neuroscience 164, 832-841
    • (2009) Neuroscience , vol.164 , pp. 832-841
    • Guenthner, C.J.1    Bickar, D.2    Harrington, M.E.3
  • 100
    • 77952593382 scopus 로고    scopus 로고
    • Heme binding to the mammalian circadian clock protein period 2 is non-specific
    • Airola, M. V., Du, J., Dawson, J. H., and Crane, B. R. (2010) Heme binding to the mammalian circadian clock protein period 2 is non-specific. Biochemistry 49, 4327-4338
    • (2010) Biochemistry , vol.49 , pp. 4327-4338
    • Airola, M.V.1    Du, J.2    Dawson, J.H.3    Crane, B.R.4
  • 102
    • 84863407362 scopus 로고    scopus 로고
    • Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): Conversion from His119/Cys170 coordination to His119/His171 coordination
    • Uchida, T., Sagami, I., Shimizu, T., Ishimori, K., and Kitagawa, T. (2012) Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination. J. Inorg. Biochem. 108, 188-195
    • (2012) J. Inorg. Biochem. , vol.108 , pp. 188-195
    • Uchida, T.1    Sagami, I.2    Shimizu, T.3    Ishimori, K.4    Kitagawa, T.5
  • 104
    • 3343024625 scopus 로고    scopus 로고
    • Reciprocal regulation of haem biosynthesis and the circadian clock in mammals
    • Kaasik, K., and Lee, C. C. (2004) Reciprocal regulation of haem biosynthesis and the circadian clock in mammals. Nature 430, 467-471
    • (2004) Nature , vol.430 , pp. 467-471
    • Kaasik, K.1    Lee, C.C.2
  • 105
    • 23944476164 scopus 로고    scopus 로고
    • Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α
    • Handschin, C., Lin, J., Rhee, J., Peyer, A. K., Chin, S., Wu, P. H., Meyer, U. A., and Spiegelman, B. M. (2005) Nutritional regulation of hepatic heme biosynthesis and porphyria through PGC-1α. Cell 122, 505-515
    • (2005) Cell , vol.122 , pp. 505-515
    • Handschin, C.1    Lin, J.2    Rhee, J.3    Peyer, A.K.4    Chin, S.5    Wu, P.H.6    Meyer, U.A.7    Spiegelman, B.M.8
  • 106
    • 70349142240 scopus 로고    scopus 로고
    • Negative feedback maintenance of heme homeostasis by its receptor, Rev-erbα
    • Wu, N., Yin, L., Hanniman, E. A., Joshi, S., and Lazar, M. A. (2009) Negative feedback maintenance of heme homeostasis by its receptor, Rev-erbα. Genes Dev. 23, 2201-2209
    • (2009) Genes Dev. , vol.23 , pp. 2201-2209
    • Wu, N.1    Yin, L.2    Hanniman, E.A.3    Joshi, S.4    Lazar, M.A.5
  • 107
    • 34249275727 scopus 로고    scopus 로고
    • Transcriptional coactivator PGC-1α integrates the mammalian clock and energy metabolism
    • Liu, C., Li, S., Liu, T., Borjigin, J., and Lin, J. D. (2007) Transcriptional coactivator PGC-1α integrates the mammalian clock and energy metabolism. Nature 447, 477-481
    • (2007) Nature , vol.447 , pp. 477-481
    • Liu, C.1    Li, S.2    Liu, T.3    Borjigin, J.4    Lin, J.D.5
  • 110
    • 40149090376 scopus 로고    scopus 로고
    • Redundant function of REV-ERBα and β and non-essential role for Bmal1 cycling in transcriptional regulation of intracellular circadian rhythms
    • Liu, A. C., Tran, H. G., Zhang, E. E., Priest, A. A., Welsh, D. K., and Kay, S. A. (2008) Redundant function of REV-ERBα and β and non-essential role for Bmal1 cycling in transcriptional regulation of intracellular circadian rhythms. PLoS Genet. 4, e1000023
    • (2008) PLoS Genet. , vol.4
    • Liu, A.C.1    Tran, H.G.2    Zhang, E.E.3    Priest, A.A.4    Welsh, D.K.5    Kay, S.A.6


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