메뉴 건너뛰기




Volumn 13, Issue 12, 2014, Pages 3507-3518

Identification of novel nuclear targets of human thioredoxin 1

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; PROTON; THIOL; THIOREDOXIN 1; DISULFIDE; PSIP1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; THIOREDOXIN; TRANSCRIPTION FACTOR; TXN PROTEIN, HUMAN;

EID: 84928243524     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.040931     Document Type: Article
Times cited : (16)

References (58)
  • 2
    • 84866540615 scopus 로고    scopus 로고
    • Redox regulation of protein misfolding, mitochondrial dysfunction, synaptic damage, and cell death in neurodegenerative diseases
    • Nakamura, T., Cho, D. H., and Lipton, S. A. (2012) Redox regulation of protein misfolding, mitochondrial dysfunction, synaptic damage, and cell death in neurodegenerative diseases. Exp. Neurol. 238, 12-21
    • (2012) Exp. Neurol. , vol.238 , pp. 12-21
    • Nakamura, T.1    Cho, D.H.2    Lipton, S.A.3
  • 5
    • 32244449328 scopus 로고    scopus 로고
    • The involvement of thioredoxin and thioredoxin binding protein-2 on cellular proliferation and aging process
    • Yoshida, T., Nakamura, H., Masutani, H., and Yodoi, J. (2005) The involvement of thioredoxin and thioredoxin binding protein-2 on cellular proliferation and aging process. Ann. N. Y. Acad. Sci. 1055, 1-12
    • (2005) Ann. N. Y. Acad. Sci. , vol.1055 , pp. 1-12
    • Yoshida, T.1    Nakamura, H.2    Masutani, H.3    Yodoi, J.4
  • 6
    • 0033618398 scopus 로고    scopus 로고
    • Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression
    • Nishiyama, A., Matsui, M., Iwata, S., Hirota, K., Masutani, H., Nakamura, H., Takagi, Y., Sono, H., Gon, Y., and Yodoi, J. (1999) Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression. J. Biol. Chem. 274, 21645-21650
    • (1999) J. Biol. Chem. , vol.274 , pp. 21645-21650
    • Nishiyama, A.1    Matsui, M.2    Iwata, S.3    Hirota, K.4    Masutani, H.5    Nakamura, H.6    Takagi, Y.7    Sono, H.8    Gon, Y.9    Yodoi, J.10
  • 8
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • Makino, Y., Yoshikawa, N., Okamoto, K., Hirota, K., Yodoi, J., Makino, I., and Tanaka, H. (1999) Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem. 274, 3182-3188
    • (1999) J. Biol. Chem. , vol.274 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 9
    • 40949111340 scopus 로고    scopus 로고
    • SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
    • Li, X., Luo, Y., Yu, L., Lin, Y., Luo, D., Zhang, H., He, Y., Kim, Y. O., Kim, Y., Tang, S., and Min, W. (2008) SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis. Cell Death Differ. 15, 739-750
    • (2008) Cell Death Differ. , vol.15 , pp. 739-750
    • Li, X.1    Luo, Y.2    Yu, L.3    Lin, Y.4    Luo, D.5    Zhang, H.6    He, Y.7    Kim, Y.O.8    Kim, Y.9    Tang, S.10    Min, W.11
  • 10
    • 4444335186 scopus 로고    scopus 로고
    • Thioredoxin as a neurotrophic cofactor and an important regulator of neuroprotection
    • Masutani, H., Bai, J., Kim, Y. C., and Yodoi, J. (2004) Thioredoxin as a neurotrophic cofactor and an important regulator of neuroprotection. Mol. Neurobiol. 29, 229-242
    • (2004) Mol. Neurobiol. , vol.29 , pp. 229-242
    • Masutani, H.1    Bai, J.2    Kim, Y.C.3    Yodoi, J.4
  • 11
    • 2642579153 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein controls cardiac hypertrophy through regulation of thioredoxin activity
    • Yoshioka, J., Schulze, P. C., Cupesi, M., Sylvan, J. D., MacGillivray, C., Gannon, J., Huang, H., and Lee, R. T. (2004) Thioredoxin-interacting protein controls cardiac hypertrophy through regulation of thioredoxin activity. Circulation 109, 2581-2586
    • (2004) Circulation , vol.109 , pp. 2581-2586
    • Yoshioka, J.1    Schulze, P.C.2    Cupesi, M.3    Sylvan, J.D.4    MacGillivray, C.5    Gannon, J.6    Huang, H.7    Lee, R.T.8
  • 12
    • 79957942591 scopus 로고    scopus 로고
    • Depletion of cytosolic or mitochondrial thioredoxin increases CYP2E1-induced oxidative stress via an ASK-1-JNK1 pathway in HepG2 cells
    • Yang, L., Wu, D., Wang, X., and Cederbaum, A. I. (2011) Depletion of cytosolic or mitochondrial thioredoxin increases CYP2E1-induced oxidative stress via an ASK-1-JNK1 pathway in HepG2 cells. Free Radic. Biol. Med. 51, 185-196
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 185-196
    • Yang, L.1    Wu, D.2    Wang, X.3    Cederbaum, A.I.4
  • 13
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin
    • Hayashi, T., Ueno, Y., and Okamoto, T. (1993) Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem. 268, 11380-11388
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 14
    • 44649184557 scopus 로고    scopus 로고
    • A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy
    • Ago, T., Liu, T., Zhai, P., Chen, W., Li, H., Molkentin, J. D., Vatner, S. F., and Sadoshima, J. (2008) A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy. Cell 133, 978-993
    • (2008) Cell , vol.133 , pp. 978-993
    • Ago, T.1    Liu, T.2    Zhai, P.3    Chen, W.4    Li, H.5    Molkentin, J.D.6    Vatner, S.F.7    Sadoshima, J.8
  • 17
    • 0347986778 scopus 로고    scopus 로고
    • Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy
    • Yamamoto, M., Yang, G., Hong, C., Liu, J., Holle, E., Yu, X., Wagner, T., Vatner, S. F., and Sadoshima, J. (2003) Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy. J. Clin. Invest. 112, 1395-1406
    • (2003) J. Clin. Invest. , vol.112 , pp. 1395-1406
    • Yamamoto, M.1    Yang, G.2    Hong, C.3    Liu, J.4    Holle, E.5    Yu, X.6    Wagner, T.7    Vatner, S.F.8    Sadoshima, J.9
  • 19
    • 77955576782 scopus 로고    scopus 로고
    • Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach
    • Benhar, M., Thompson, J. W., Moseley, M. A., and Stamler, J. S. (2010) Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry 49, 6963-6969
    • (2010) Biochemistry , vol.49 , pp. 6963-6969
    • Benhar, M.1    Thompson, J.W.2    Moseley, M.A.3    Stamler, J.S.4
  • 20
    • 84878238118 scopus 로고    scopus 로고
    • A multidimensional approach to an in-depth proteomics analysis of transcriptional regulators in neuroblastoma cells
    • Li, Q., Jain, M. R., Chen, W., and Li, H. (2013) A multidimensional approach to an in-depth proteomics analysis of transcriptional regulators in neuroblastoma cells. J. Neurosci. Methods 216, 118-127
    • (2013) J. Neurosci. Methods , vol.216 , pp. 118-127
    • Li, Q.1    Jain, M.R.2    Chen, W.3    Li, H.4
  • 22
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 23
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 24
    • 11244255412 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase
    • Llano, M., Delgado, S., Vanegas, M., and Poeschla, E. M. (2004) Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase. J. Biol. Chem. 279, 55570-55577
    • (2004) J. Biol. Chem. , vol.279 , pp. 55570-55577
    • Llano, M.1    Delgado, S.2    Vanegas, M.3    Poeschla, E.M.4
  • 25
    • 0033538442 scopus 로고    scopus 로고
    • In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family
    • Verdoucq, L., Vignols, F., Jacquot, J. P., Chartier, Y., and Meyer, Y. (1999) In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J. Biol. Chem. 274, 19714-19722
    • (1999) J. Biol. Chem. , vol.274 , pp. 19714-19722
    • Verdoucq, L.1    Vignols, F.2    Jacquot, J.P.3    Chartier, Y.4    Meyer, Y.5
  • 28
    • 1642371610 scopus 로고    scopus 로고
    • Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts
    • Balmer, Y., Koller, A., Val, G. D., Schurmann, P., and Buchanan, B. B. (2004) Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynthesis Res. 79, 275-280
    • (2004) Photosynthesis Res , vol.79 , pp. 275-280
    • Balmer, Y.1    Koller, A.2    Val, G.D.3    Schurmann, P.4    Buchanan, B.B.5
  • 34
    • 12744274638 scopus 로고    scopus 로고
    • Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses
    • Rey, P., Cuine, S., Eymery, F., Garin, J., Court, M., Jacquot, J. P., Rouhier, N., and Broin, M. (2005) Analysis of the proteins targeted by CDSP32, a plastidic thioredoxin participating in oxidative stress responses. Plant J. 41, 31-42
    • (2005) Plant J , vol.41 , pp. 31-42
    • Rey, P.1    Cuine, S.2    Eymery, F.3    Garin, J.4    Court, M.5    Jacquot, J.P.6    Rouhier, N.7    Broin, M.8
  • 36
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding
    • Kadokura, H., Tian, H., Zander, T., Bardwell, J. C., and Beckwith, J. (2004) Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 303, 534-537
    • (2004) Science , vol.303 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.4    Beckwith, J.5
  • 37
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar, J. K., Tabor, S., and Richardson, C. C. (2004) Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 101, 3759-3764
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 38
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J. H., Balmer, Y., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. (2003) Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 547, 151-156
    • (2003) FEBS Lett , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4    Vensel, W.H.5    Hurkman, W.J.6    Buchanan, B.B.7
  • 39
    • 2342597074 scopus 로고    scopus 로고
    • Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: An early event in cereal germination
    • Wong, J. H., Cai, N., Tanaka, C. K., Vensel, W. H., Hurkman, W. J., and Buchanan, B. B. (2004) Thioredoxin reduction alters the solubility of proteins of wheat starchy endosperm: an early event in cereal germination. Plant Cell Physiol. 45, 407-415
    • (2004) Plant Cell Physiol , vol.45 , pp. 407-415
    • Wong, J.H.1    Cai, N.2    Tanaka, C.K.3    Vensel, W.H.4    Hurkman, W.J.5    Buchanan, B.B.6
  • 40
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. Strain PCC 6803
    • Hosoya-Matsuda, N., Motohashi, K., Yoshimura, H., Nozaki, A., Inoue, K., Ohmori, M., and Hisabori, T. (2005) Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. J. Biol. Chem. 280, 840-846
    • (2005) J. Biol. Chem. , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6    Hisabori, T.7
  • 41
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl, M., and Florencio, F. J. (2003) Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc. Natl. Acad. Sci. U.S.A. 100, 16107-16112
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 16107-16112
    • Lindahl, M.1    Florencio, F.J.2
  • 42
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • Mata-Cabana, A., Florencio, F. J., and Lindahl, M. (2007) Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics 7, 3953-3963
    • (2007) Proteomics , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, M.3
  • 43
    • 80054870283 scopus 로고    scopus 로고
    • Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach
    • Wu, C., Parrott, A. M., Liu, T., Jain, M. R., Yang, Y., Sadoshima, J., and Li, H. (2011) Distinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach. J. Proteomics 74, 2498-2509
    • (2011) J. Proteomics , vol.74 , pp. 2498-2509
    • Wu, C.1    Parrott, A.M.2    Liu, T.3    Jain, M.R.4    Yang, Y.5    Sadoshima, J.6    Li, H.7
  • 44
    • 61349103096 scopus 로고    scopus 로고
    • Identification of thioredoxin disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags
    • Hagglund, P., Bunkenborg, J., Maeda, K., and Svensson, B. (2008) Identification of thioredoxin disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags. J. Proteome Res. 7, 5270-5276
    • (2008) J. Proteome Res. , vol.7 , pp. 5270-5276
    • Hagglund, P.1    Bunkenborg, J.2    Maeda, K.3    Svensson, B.4
  • 45
    • 33748794796 scopus 로고    scopus 로고
    • Autoantibodies to p75/LEDGF, a cell survival factor, found in patients with atypical retinal degeneration
    • Chin, M. S., Caruso, R. C., Detrick, B., and Hooks, J. J. (2006) Autoantibodies to p75/LEDGF, a cell survival factor, found in patients with atypical retinal degeneration. J. Autoimmun. 27, 17-27
    • (2006) J. Autoimmun. , vol.27 , pp. 17-27
    • Chin, M.S.1    Caruso, R.C.2    Detrick, B.3    Hooks, J.J.4
  • 47
    • 0033967955 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing
    • Singh, D. P., Kimura, A., Chylack, L. T., Jr., and Shinohara, T. (2000) Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing. Gene 242, 265-273
    • (2000) Gene , vol.242 , pp. 265-273
    • Singh, D.P.1    Kimura, A.2    Chylack, L.T.3    Shinohara, T.4
  • 49
    • 0032976273 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor: Increased resistance to thermal and oxidative stresses
    • Singh, D. P., Ohguro, N., Chylack, L. T., Jr., and Shinohara, T. (1999) Lens epithelium-derived growth factor: increased resistance to thermal and oxidative stresses. Invest. Ophthalmol. Vis. Sci. 40, 1444-1451
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 1444-1451
    • Singh, D.P.1    Ohguro, N.2    Chylack, L.T.3    Shinohara, T.4
  • 50
    • 21744436817 scopus 로고    scopus 로고
    • Impaired homeostasis and phenotypic abnormalities in Prdx6-/-mice lens epithelial cells by reactive oxygen species: Increased expression and activation of TGFbeta
    • Fatma, N., Kubo, E., Sharma, P., Beier, D. R., and Singh, D. P. (2005) Impaired homeostasis and phenotypic abnormalities in Prdx6-/-mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFbeta. Cell Death Differ. 12, 734-750
    • (2005) Cell Death Differ , vol.12 , pp. 734-750
    • Fatma, N.1    Kubo, E.2    Sharma, P.3    Beier, D.R.4    Singh, D.P.5
  • 51
    • 32444439020 scopus 로고    scopus 로고
    • Transient and stable knockdown of the integrase cofactor LEDGF/p75 reveals its role in the replication cycle of human immunodeficiency virus
    • Vandekerckhove, L., Christ, F., Van Maele, B., De Rijck, J., Gijsbers, R., Van den Haute, C., Witvrouw, M., and Debyser, Z. (2006) Transient and stable knockdown of the integrase cofactor LEDGF/p75 reveals its role in the replication cycle of human immunodeficiency virus. J. Virol. 80, 1886-1896
    • (2006) J. Virol. , vol.80 , pp. 1886-1896
    • Vandekerckhove, L.1    Christ, F.2    Van Maele, B.3    De Rijck, J.4    Gijsbers, R.5    Van Den Haute, C.6    Witvrouw, M.7    Debyser, Z.8
  • 54
    • 84870670336 scopus 로고    scopus 로고
    • The LEDGF/p75 integrase interaction, a novel target for anti-HIV therapy
    • Christ, F., and Debyser, Z. (2013) The LEDGF/p75 integrase interaction, a novel target for anti-HIV therapy. Virology 435, 102-109
    • (2013) Virology , vol.435 , pp. 102-109
    • Christ, F.1    Debyser, Z.2
  • 55
    • 31944432877 scopus 로고    scopus 로고
    • The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma
    • Baker, A. F., Dragovich, T., Tate, W. R., Ramanathan, R. K., Roe, D., Hsu, C. H., Kirkpatrick, D. L., and Powis, G. (2006) The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma. J. Lab. Clin. Med. 147, 83-90
    • (2006) J. Lab. Clin. Med. , vol.147 , pp. 83-90
    • Baker, A.F.1    Dragovich, T.2    Tate, W.R.3    Ramanathan, R.K.4    Roe, D.5    Hsu, C.H.6    Kirkpatrick, D.L.7    Powis, G.8
  • 56
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo, M. A., Raices, M., Panowski, S. H., and Hetzer, M. W. (2009) Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 136, 284-295
    • (2009) Cell , vol.136 , pp. 284-295
    • D'Angelo, M.A.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 57
    • 84880666472 scopus 로고    scopus 로고
    • Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport
    • Yoshimura, S. H., Otsuka, S., Kumeta, M., Taga, M., and Takeyasu, K. (2013) Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport. J. Cell Sci. 126, 3141-3150
    • (2013) J. Cell Sci. , vol.126 , pp. 3141-3150
    • Yoshimura, S.H.1    Otsuka, S.2    Kumeta, M.3    Taga, M.4    Takeyasu, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.