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Volumn 7, Issue 3-4, 2005, Pages 303-307

Redox control of protein trafficking

Author keywords

[No Author keywords available]

Indexed keywords

REACTIVE OXYGEN METABOLITE;

EID: 14044279872     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2005.7.303     Document Type: Editorial
Times cited : (3)

References (47)
  • 1
    • 0035889083 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton
    • Aplin AE and Juliano RL. Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton. J Cell Biol 155: 187-191, 2001.
    • (2001) J Cell Biol , vol.155 , pp. 187-191
    • Aplin, A.E.1    Juliano, R.L.2
  • 2
    • 14044250859 scopus 로고    scopus 로고
    • Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels
    • Arrigo A-P, Virot S, Chaufour S, Firdaus W, Kretz-Remy C, and Diaz-Latoud C. Hsp27 consolidates intracellular redox homeostasis by upholding glutathione in its reduced form and by decreasing iron intracellular levels. Antioxid Redox Signal 7: 414-424, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 414-424
    • Arrigo, A.-P.1    Virot, S.2    Chaufour, S.3    Firdaus, W.4    Kretz-Remy, C.5    Diaz-Latoud, C.6
  • 3
    • 0037084009 scopus 로고    scopus 로고
    • Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress
    • Blanchetot C, Tertoolen LG, and den Hertog J. Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress. EMBO J 21: 493-503, 2002.
    • (2002) EMBO J , vol.21 , pp. 493-503
    • Blanchetot, C.1    Tertoolen, L.G.2    Den Hertog, J.3
  • 6
    • 0035877590 scopus 로고    scopus 로고
    • The regulation of nuclear localization during signal transduction
    • Cyert MS. The regulation of nuclear localization during signal transduction. J Biol Chem 276: 20805-20808, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 20805-20808
    • Cyert, M.S.1
  • 7
    • 0028942661 scopus 로고
    • Involvement of reactive oxygen intermediates in cyclooxygenase-2 expression induced by interleukin-1, tumor necrosis factor-alpha, and lipopolysaccharide
    • Feng L, Zia Y, Garcia GE, Hwang D, and Wilson CB. Involvement of reactive oxygen intermediates in cyclooxygenase-2 expression induced by interleukin-1, tumor necrosis factor-alpha, and lipopolysaccharide. J Clin Invest 95: 1669-1675, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 1669-1675
    • Feng, L.1    Zia, Y.2    Garcia, G.E.3    Hwang, D.4    Wilson, C.B.5
  • 8
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel T. Oxidant signals and oxidative stress. Curr Opin Cell Biol 15: 247-254, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 247-254
    • Finkel, T.1
  • 9
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D and Kutay U. Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 15: 607-660, 1999.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 10
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase. Role in cardiovascular biology and disease
    • Griendling KK, Sorescu D, and Ushio-Fukai M. NAD(P)H oxidase. Role in cardiovascular biology and disease. Circ Res 86: 494-501, 2000.
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 11
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J, Houle F, Marceau F, and Landry J. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ Res 80: 383-392, 1997.
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 12
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-κB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y, Ando K, Hirao S, Yoshida M, and Handa H. Redox regulation of NF-κB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 7: 395-403, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 13
    • 0032496326 scopus 로고    scopus 로고
    • Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change
    • Kheradmand F, Werner E, Tremble P, Symons M, and Werb Z. Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280: 898-902, 1998.
    • (1998) Science , vol.280 , pp. 898-902
    • Kheradmand, F.1    Werner, E.2    Tremble, P.3    Symons, M.4    Werb, Z.5
  • 14
    • 14044254798 scopus 로고    scopus 로고
    • Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation
    • Kobayashi M and Yamamoto M. Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation. Antioxid Redox Signal 7: 385-394, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 385-394
    • Kobayashi, M.1    Yamamoto, M.2
  • 15
    • 0033591412 scopus 로고    scopus 로고
    • A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Papl
    • Kudo N, Taoka H, Toda T, Yoshida M, and Horinouchi S. A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Papl. J Biol Chem 274: 15151-15158, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 15151-15158
    • Kudo, N.1    Taoka, H.2    Toda, T.3    Yoshida, M.4    Horinouchi, S.5
  • 16
    • 0030942294 scopus 로고    scopus 로고
    • Regulation of yAP-1 nuclear localization in response to oxidative stress
    • Kuge S, Jones N, and Nomoto A. Regulation of yAP-1 nuclear localization in response to oxidative stress. EMBO J 16: 1710-1720, 1997.
    • (1997) EMBO J , vol.16 , pp. 1710-1720
    • Kuge, S.1    Jones, N.2    Nomoto, A.3
  • 17
    • 0042810670 scopus 로고    scopus 로고
    • Vascular NAD(P)H oxidases: Specific features, expression, and regulation
    • Lassegue B and Clempus RE. Vascular NAD(P)H oxidases: specific features, expression, and regulation. Am J Physiol Regul Integr Comp Physiol 285: R277-R297, 2003.
    • (2003) Am J Physiol Regul Integr Comp Physiol , vol.285
    • Lassegue, B.1    Clempus, R.E.2
  • 18
    • 0032429751 scopus 로고    scopus 로고
    • Communication between the cell membrane and the nucleus: Role of protein compartmentalization
    • Lelievre SA and Bissell MJ. Communication between the cell membrane and the nucleus: role of protein compartmentalization. J Cell Biochem Suppl 30/31: 250-263, 1998.
    • (1998) J Cell Biochem Suppl , vol.30-31 , pp. 250-263
    • Lelievre, S.A.1    Bissell, M.J.2
  • 19
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Lo YY and Cruz TF. Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J Biol Chem 270: 11727-11730, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1    Cruz, T.F.2
  • 20
    • 0024425516 scopus 로고
    • Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha
    • Meier B, Radeke HH, Selle S, Younes M, Sie H, Resch K, and Habermehl G.G. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-alpha. Biochem J 263: 539-545, 1989.
    • (1989) Biochem J , vol.263 , pp. 539-545
    • Meier, B.1    Radeke, H.H.2    Selle, S.3    Younes, M.4    Sie, H.5    Resch, K.6    Habermehl, G.G.7
  • 21
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng TC, Fukada T, and Tonks NK. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol Cell 9: 387-399, 2002.
    • (2002) Mol Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 22
    • 0033965904 scopus 로고    scopus 로고
    • CIZ, a zinc finger protein that interacts with p130(cas) and activates the expression of matrix metalloproteinases
    • Nakamoto T, Yamagata T, Sakai R, Ogawa S, Honda H, Ueno H, Hirano N, Yazaki Y, and Hirai H. CIZ, a zinc finger protein that interacts with p130(cas) and activates the expression of matrix metalloproteinases. Mol Cell Biol 20: 1649-1658, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 1649-1658
    • Nakamoto, T.1    Yamagata, T.2    Sakai, R.3    Ogawa, S.4    Honda, H.5    Ueno, H.6    Hirano, N.7    Yazaki, Y.8    Hirai, H.9
  • 23
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: A potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix DA and Beckerle MC. Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J Cell Biol 138: 1139-1147, 1997.
    • (1997) J Cell Biol , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 25
    • 0028015832 scopus 로고
    • Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells
    • Ohba M, Shibanuma M, Kuroki T, and Nose K. Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells. J Cell Biol 126: 1079-1088, 1994.
    • (1994) J Cell Biol , vol.126 , pp. 1079-1088
    • Ohba, M.1    Shibanuma, M.2    Kuroki, T.3    Nose, K.4
  • 26
    • 14044271510 scopus 로고    scopus 로고
    • Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast
    • Okazaki S, Naganuma A, and Kuge S. Peroxiredoxin-mediated redox regulation of the nuclear localization of Yap1, a transcription factor in budding yeast. Antioxid Redox Signal 7: 327-334, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 327-334
    • Okazaki, S.1    Naganuma, A.2    Kuge, S.3
  • 29
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2 A by hydrogen peroxide and glutathionylation. B
    • Rao RK and Clayton LW. Regulation of protein phosphatase 2 A by hydrogen peroxide and glutathionylation. Biochem Biophys Res Commun 293: 610-616, 2002.
    • (2002) Iochem Biophys Res Commun , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 31
    • 0027301258 scopus 로고
    • Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase
    • Satoriano JA, Shuldiner M, Hora K, Zing Y, Shan Z, and Schlondorff DJ. Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase. Clin Invest 92: 1564-1571, 1993.
    • (1993) Clin Invest , vol.92 , pp. 1564-1571
    • Satoriano, J.A.1    Shuldiner, M.2    Hora, K.3    Zing, Y.4    Shan, Z.5    Schlondorff, D.J.6
  • 32
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation
    • Shelton MD, Chock PB, and Mieyal JJ. Glutaredoxin: role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 7: 348-366, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 33
    • 0023194380 scopus 로고
    • Effects of the protein kinase C inhibitor H-7 and calmodulin antagonist W-7 on superoxide production in growing and resting human histiocytic leukemia cells (U937)
    • Shibanuma M, Kuroki T, and Nose K. Effects of the protein kinase C inhibitor H-7 and calmodulin antagonist W-7 on superoxide production in growing and resting human histiocytic leukemia cells (U937). Biochem Biophys Res Commun 144: 1317-1323, 1987.
    • (1987) Biochem Biophys Res Commun , vol.144 , pp. 1317-1323
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 34
    • 0026248489 scopus 로고
    • 2 and phosphorylation of 30 kilodalton proteins as early responses of cell cycle-dependent inhibition of DNA synthesis by transforming growth factor beta 1
    • 2 and phosphorylation of 30 kilodalton proteins as early responses of cell cycle-dependent inhibition of DNA synthesis by transforming growth factor beta 1. Cell Growth Differ 2: 583-591, 1991.
    • (1991) Cell Growth Differ , vol.2 , pp. 583-591
    • Shibanuma, M.1    Kuroki, T.2    Nose, K.3
  • 35
    • 0037345037 scopus 로고    scopus 로고
    • Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal
    • Shibanuma M, Kim-Kaneyama J, Sato S, Ishino K, Sakamoto N, Mashimo J, and Nose K. Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal. Mol Biol Cell 14: 1158-1171, 2003.
    • (2003) Mol Biol Cell , vol.14 , pp. 1158-1171
    • Shibanuma, M.1    Kim-Kaneyama, J.2    Sato, S.3    Ishino, K.4    Sakamoto, N.5    Mashimo, J.6    Nose, K.7
  • 36
    • 3843126775 scopus 로고    scopus 로고
    • A L1M protein, Hic-5, functions as a potential coactivator for Sp1
    • Shibanuma M, Kim-Kaneyama J, Sato S, and Nose K. A L1M protein, Hic-5, functions as a potential coactivator for Sp1. J Cell Biochem 15: 633-645, 2003.
    • (2003) J Cell Biochem , vol.15 , pp. 633-645
    • Shibanuma, M.1    Kim-Kaneyama, J.2    Sato, S.3    Nose, K.4
  • 37
    • 14044273001 scopus 로고    scopus 로고
    • Involvement of FAK and PTP-PEST in the regulation of redox-sensitive nuclear-cytoplasmic shuttling of a LIM protein, Hic-5
    • Shibanuma M, Mori K, Kim-Kaneyama J, and Nose K. Involvement of FAK and PTP-PEST in the regulation of redox-sensitive nuclear-cytoplasmic shuttling of a LIM protein, Hic-5. Antioxid Redox Signal 7: 335-347, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 335-347
    • Shibanuma, M.1    Mori, K.2    Kim-Kaneyama, J.3    Nose, K.4
  • 39
    • 14044268133 scopus 로고    scopus 로고
    • Essential roles of lipoxygenases in LDL oxidation and development of atherosclerosis
    • Takahashi Y, Zhu H, and Yoshimoto T. Essential roles of lipoxygenases in LDL oxidation and development of atherosclerosis. Antioxid Redox Signal 7: 425-431, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 425-431
    • Takahashi, Y.1    Zhu, H.2    Yoshimoto, T.3
  • 40
    • 14044269479 scopus 로고    scopus 로고
    • The intracellular localization of APE1/Ref-1: More than a passive phenomenon?
    • Tell G, Damante G, Caldwell D, and Kelley MR. The intracellular localization of APE1/Ref-1: more than a passive phenomenon? Antioxid Redox Signal 7: 367-384, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 367-384
    • Tell, G.1    Damante, G.2    Caldwell, D.3    Kelley, M.R.4
  • 41
    • 0033060357 scopus 로고    scopus 로고
    • Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin
    • Thomas SM, Hagel M, and Turner CE. Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin. J Cell Sci 112: 181-190, 1999.
    • (1999) J Cell Sci , vol.112 , pp. 181-190
    • Thomas, S.M.1    Hagel, M.2    Turner, C.E.3
  • 42
    • 0032523783 scopus 로고    scopus 로고
    • Regulation of the fission yeast transcription factor Pap1 by oxidative stress: Requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAPkinase Sty1/Spc1
    • Toone WM, Kuge S, Samuels M, Morgan BA, Toda T, and Jones N. Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (exportin) and the stress-activated MAPkinase Sty1/Spc1. Genes Dev 12: 1453-1463, 1998.
    • (1998) Genes Dev , vol.12 , pp. 1453-1463
    • Toone, W.M.1    Kuge, S.2    Samuels, M.3    Morgan, B.A.4    Toda, T.5    Jones, N.6
  • 44
    • 0035938201 scopus 로고    scopus 로고
    • LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains
    • Wang Y and Gilmore TD. LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains. Biochim Biophys Acta 1538: 260-272, 2001.
    • (2001) Biochim Biophys Acta , vol.1538 , pp. 260-272
    • Wang, Y.1    Gilmore, T.D.2
  • 45
    • 14044264196 scopus 로고    scopus 로고
    • Integrin clustering drives phagocytosis coupled to collagenase 1 induction through RhoA GTPase and superoxide production
    • Werner E. Integrin clustering drives phagocytosis coupled to collagenase 1 induction through RhoA GTPase and superoxide production. Antioxid Redox Signal 7: 318-326, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 318-326
    • Werner, E.1
  • 47
    • 0033625751 scopus 로고    scopus 로고
    • Interaction of the τ2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix
    • Yang L, Guerrero J, Hong H, DeFranco DB, and Stallcup MR. Interaction of the τ2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix. Mol Biol Cell 11: 2007-2018, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 2007-2018
    • Yang, L.1    Guerrero, J.2    Hong, H.3    DeFranco, D.B.4    Stallcup, M.R.5


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