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Volumn 52, Issue 1, 2013, Pages 75-86

SOD1 as a molecular switch for initiating the homeostatic ER stress response under zinc deficiency

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; DERLIN 1; MUTANT PROTEIN; UNCLASSIFIED DRUG; ZINC; ZINC TRANSPORTER;

EID: 84885382830     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.08.038     Document Type: Article
Times cited : (108)

References (51)
  • 2
    • 43049150678 scopus 로고    scopus 로고
    • Metals in Alzheimer's and Parkinson's diseases
    • Barnham K.J., Bush A.I. Metals in Alzheimer's and Parkinson's diseases. Curr. Opin. Chem. Biol. 2008, 12:222-228.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 222-228
    • Barnham, K.J.1    Bush, A.I.2
  • 3
    • 4043075622 scopus 로고    scopus 로고
    • Lessons from models of SOD1-linked familial ALS
    • Bendotti C., Carrì M.T. Lessons from models of SOD1-linked familial ALS. Trends Mol. Med. 2004, 10:393-400.
    • (2004) Trends Mol. Med. , vol.10 , pp. 393-400
    • Bendotti, C.1    Carrì, M.T.2
  • 5
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J.P., Sampson J.B., Zhuang Y., Thompson J.A., Beckman J.S. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J.Neurochem. 1997, 69:1936-1944.
    • (1997) J.Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.3    Thompson, J.A.4    Beckman, J.S.5
  • 7
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng H.X., Shi Y., Furukawa Y., Zhai H., Fu R., Liu E., Gorrie G.H., Khan M.S., Hung W.Y., Bigio E.H., et al. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc. Natl. Acad. Sci. USA 2006, 103:7142-7147.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7142-7147
    • Deng, H.X.1    Shi, Y.2    Furukawa, Y.3    Zhai, H.4    Fu, R.5    Liu, E.6    Gorrie, G.H.7    Khan, M.S.8    Hung, W.Y.9    Bigio, E.H.10
  • 8
    • 3543109122 scopus 로고    scopus 로고
    • Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function
    • Ellis C.D., Wang F., MacDiarmid C.W., Clark S., Lyons T., Eide D.J. Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function. J.Cell Biol. 2004, 166:325-335.
    • (2004) J.Cell Biol. , vol.166 , pp. 325-335
    • Ellis, C.D.1    Wang, F.2    MacDiarmid, C.W.3    Clark, S.4    Lyons, T.5    Eide, D.J.6
  • 10
    • 0015935503 scopus 로고
    • On the stability of bovine superoxide dismutase. The effects of metals
    • Forman H.J., Fridovich I. On the stability of bovine superoxide dismutase. The effects of metals. J.Biol. Chem. 1973, 248:2645-2649.
    • (1973) J.Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 14
    • 0037013264 scopus 로고    scopus 로고
    • Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
    • Hayward L.J., Rodriguez J.A., Kim J.W., Tiwari A., Goto J.J., Cabelli D.E., Valentine J.S., Brown R.H. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. J.Biol. Chem. 2002, 277:15923-15931.
    • (2002) J.Biol. Chem. , vol.277 , pp. 15923-15931
    • Hayward, L.J.1    Rodriguez, J.A.2    Kim, J.W.3    Tiwari, A.4    Goto, J.J.5    Cabelli, D.E.6    Valentine, J.S.7    Brown, R.H.8
  • 15
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K., Yoshida H., Yanagi H., Yura T., Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 1999, 10:3787-3799.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 16
    • 79952977920 scopus 로고    scopus 로고
    • The zinc transporter SLC39A14/ZIP14 controls G-protein coupled receptor-mediated signaling required for systemic growth
    • Hojyo S., Fukada T., Shimoda S., Ohashi W., Bin B.H., Koseki H., Hirano T. The zinc transporter SLC39A14/ZIP14 controls G-protein coupled receptor-mediated signaling required for systemic growth. PLoS ONE 2011, 6:e18059.
    • (2011) PLoS ONE , vol.6
    • Hojyo, S.1    Fukada, T.2    Shimoda, S.3    Ohashi, W.4    Bin, B.H.5    Koseki, H.6    Hirano, T.7
  • 17
    • 74049164709 scopus 로고    scopus 로고
    • Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond
    • Ilieva H., Polymenidou M., Cleveland D.W. Non-cell autonomous toxicity in neurodegenerative disorders: ALS and beyond. J.Cell Biol. 2009, 187:761-772.
    • (2009) J.Cell Biol. , vol.187 , pp. 761-772
    • Ilieva, H.1    Polymenidou, M.2    Cleveland, D.W.3
  • 18
    • 33745842537 scopus 로고    scopus 로고
    • Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells
    • Ishihara K., Yamazaki T., Ishida Y., Suzuki T., Oda K., Nagao M., Yamaguchi-Iwai Y., Kambe T. Zinc transport complexes contribute to the homeostatic maintenance of secretory pathway function in vertebrate cells. J.Biol. Chem. 2006, 281:17743-17750.
    • (2006) J.Biol. Chem. , vol.281 , pp. 17743-17750
    • Ishihara, K.1    Yamazaki, T.2    Ishida, Y.3    Suzuki, T.4    Oda, K.5    Nagao, M.6    Yamaguchi-Iwai, Y.7    Kambe, T.8
  • 19
    • 0023925758 scopus 로고
    • Trace elements in human clinical specimens: evaluation of literature data to identify reference values
    • Iyengar V., Woittiez J. Trace elements in human clinical specimens: evaluation of literature data to identify reference values. Clin. Chem. 1988, 34:474-481.
    • (1988) Clin. Chem. , vol.34 , pp. 474-481
    • Iyengar, V.1    Woittiez, J.2
  • 20
    • 57049117856 scopus 로고    scopus 로고
    • Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities
    • Kim I., Xu W., Reed J.C. Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities. Nat. Rev. Drug Discov. 2008, 7:1013-1030.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 1013-1030
    • Kim, I.1    Xu, W.2    Reed, J.C.3
  • 21
    • 64449085918 scopus 로고    scopus 로고
    • Accumulation of labile zinc in neurons and astrocytes in the spinal cords of G93A SOD-1 transgenic mice
    • Kim J., Kim T.Y., Hwang J.J., Lee J.Y., Shin J.H., Gwag B.J., Koh J.Y. Accumulation of labile zinc in neurons and astrocytes in the spinal cords of G93A SOD-1 transgenic mice. Neurobiol. Dis. 2009, 34:221-229.
    • (2009) Neurobiol. Dis. , vol.34 , pp. 221-229
    • Kim, J.1    Kim, T.Y.2    Hwang, J.J.3    Lee, J.Y.4    Shin, J.H.5    Gwag, B.J.6    Koh, J.Y.7
  • 23
    • 67149099224 scopus 로고    scopus 로고
    • Interleukin-1beta contributes via nitric oxide to the upregulation and functional activity of the zinc transporter Zip14 (Slc39a14) in murine hepatocytes
    • Lichten L.A., Liuzzi J.P., Cousins R.J. Interleukin-1beta contributes via nitric oxide to the upregulation and functional activity of the zinc transporter Zip14 (Slc39a14) in murine hepatocytes. Am. J. Physiol. Gastrointest. Liver Physiol. 2009, 296:G860-G867.
    • (2009) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.296
    • Lichten, L.A.1    Liuzzi, J.P.2    Cousins, R.J.3
  • 24
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004, 429:834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 26
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 2007, 18:716-731.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 27
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak S.J., Ron D. Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 2006, 86:1133-1149.
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 30
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
    • Niwa J., Yamada S., Ishigaki S., Sone J., Takahashi M., Katsuno M., Tanaka F., Doyu M., Sobue G. Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. J.Biol. Chem. 2007, 282:28087-28095.
    • (2007) J.Biol. Chem. , vol.282 , pp. 28087-28095
    • Niwa, J.1    Yamada, S.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5    Katsuno, M.6    Tanaka, F.7    Doyu, M.8    Sobue, G.9
  • 31
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • Pardo C.A., Xu Z., Borchelt D.R., Price D.L., Sisodia S.S., Cleveland D.W. Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc. Natl. Acad. Sci. USA 1995, 92:954-958.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5    Cleveland, D.W.6
  • 32
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli P., Brown R.H. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat. Rev. Neurosci. 2006, 7:710-723.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 33
    • 84859512071 scopus 로고    scopus 로고
    • Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis
    • Pokrishevsky E., Grad L.I., Yousefi M., Wang J., Mackenzie I.R., Cashman N.R. Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis. PLoS ONE 2012, 7:e35050.
    • (2012) PLoS ONE , vol.7
    • Pokrishevsky, E.1    Grad, L.I.2    Yousefi, M.3    Wang, J.4    Mackenzie, I.R.5    Cashman, N.R.6
  • 34
    • 44649133156 scopus 로고    scopus 로고
    • Zinc in human health: effect of zinc on immune cells
    • Prasad A.S. Zinc in human health: effect of zinc on immune cells. Mol. Med. 2008, 14:353-357.
    • (2008) Mol. Med. , vol.14 , pp. 353-357
    • Prasad, A.S.1
  • 35
    • 0037109771 scopus 로고    scopus 로고
    • Disease progression in a transgenic model of familial amyotrophic lateral sclerosis is dependent on both neuronal and non-neuronal zinc binding proteins
    • Puttaparthi K., Gitomer W.L., Krishnan U., Son M., Rajendran B., Elliott J.L. Disease progression in a transgenic model of familial amyotrophic lateral sclerosis is dependent on both neuronal and non-neuronal zinc binding proteins. J.Neurosci. 2002, 22:8790-8796.
    • (2002) J.Neurosci. , vol.22 , pp. 8790-8796
    • Puttaparthi, K.1    Gitomer, W.L.2    Krishnan, U.3    Son, M.4    Rajendran, B.5    Elliott, J.L.6
  • 37
    • 52949135993 scopus 로고    scopus 로고
    • ZIP7-mediated intracellular zinc transport contributes to aberrant growth factor signaling in antihormone-resistant breast cancer Cells
    • Taylor K.M., Vichova P., Jordan N., Hiscox S., Hendley R., Nicholson R.I. ZIP7-mediated intracellular zinc transport contributes to aberrant growth factor signaling in antihormone-resistant breast cancer Cells. Endocrinology 2008, 149:4912-4920.
    • (2008) Endocrinology , vol.149 , pp. 4912-4920
    • Taylor, K.M.1    Vichova, P.2    Jordan, N.3    Hiscox, S.4    Hendley, R.5    Nicholson, R.I.6
  • 38
    • 42249102078 scopus 로고    scopus 로고
    • Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS
    • Turner B.J., Talbot K. Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS. Prog. Neurobiol. 2008, 85:94-134.
    • (2008) Prog. Neurobiol. , vol.85 , pp. 94-134
    • Turner, B.J.1    Talbot, K.2
  • 39
    • 0018519484 scopus 로고
    • PH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase
    • Valentine J.S., Pantoliano M.W., McDonnell P.J., Burger A.R., Lippard S.J. pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase. Proc. Natl. Acad. Sci. USA 1979, 76:4245-4249.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4245-4249
    • Valentine, J.S.1    Pantoliano, M.W.2    McDonnell, P.J.3    Burger, A.R.4    Lippard, S.J.5
  • 40
    • 0027466337 scopus 로고
    • Cocatalytic zinc motifs in enzyme catalysis
    • Vallee B.L., Auld D.S. Cocatalytic zinc motifs in enzyme catalysis. Proc. Natl. Acad. Sci. USA 1993, 90:2715-2718.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2715-2718
    • Vallee, B.L.1    Auld, D.S.2
  • 42
    • 59149094252 scopus 로고    scopus 로고
    • Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis
    • Vonk W.I., Klomp L.W. Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis. Biochem. Soc. Trans. 2008, 36:1322-1328.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1322-1328
    • Vonk, W.I.1    Klomp, L.W.2
  • 43
    • 0035977016 scopus 로고    scopus 로고
    • Evidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism
    • Wei J.P., Srinivasan C., Han H., Valentine J.S., Gralla E.B. Evidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism. J.Biol. Chem. 2001, 276:44798-44803.
    • (2001) J.Biol. Chem. , vol.276 , pp. 44798-44803
    • Wei, J.P.1    Srinivasan, C.2    Han, H.3    Valentine, J.S.4    Gralla, E.B.5
  • 46
    • 70349487306 scopus 로고    scopus 로고
    • Cytosolic superoxide dismutase (SOD1) is critical for tolerating the oxidative stress of zinc deficiency in yeast
    • Wu C.Y., Steffen J., Eide D.J. Cytosolic superoxide dismutase (SOD1) is critical for tolerating the oxidative stress of zinc deficiency in yeast. PLoS ONE 2009, 4:e7061.
    • (2009) PLoS ONE , vol.4
    • Wu, C.Y.1    Steffen, J.2    Eide, D.J.3
  • 47
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K., Yoshida H., Kokame K., Kaufman R.J., Mori K. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J.Biochem. 2004, 136:343-350.
    • (2004) J.Biochem. , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 48
    • 84862691112 scopus 로고    scopus 로고
    • A novel role of the L-type calcium channel α1D subunit as a gatekeeper for intracellular zinc signaling: zinc wave
    • Yamasaki S., Hasegawa A., Hojyo S., Ohashi W., Fukada T., Nishida K., Hirano T. A novel role of the L-type calcium channel α1D subunit as a gatekeeper for intracellular zinc signaling: zinc wave. PLoS ONE 2012, 7:e39654.
    • (2012) PLoS ONE , vol.7
    • Yamasaki, S.1    Hasegawa, A.2    Hojyo, S.3    Ohashi, W.4    Fukada, T.5    Nishida, K.6    Hirano, T.7
  • 49
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004, 429:841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 50
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H., Haze K., Yanagi H., Yura T., Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J.Biol. Chem. 1998, 273:33741-33749.
    • (1998) J.Biol. Chem. , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 51
    • 77957783944 scopus 로고    scopus 로고
    • ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin
    • Zhao N., Gao J., Enns C.A., Knutson M.D. ZRT/IRT-like protein 14 (ZIP14) promotes the cellular assimilation of iron from transferrin. J.Biol. Chem. 2010, 285:32141-32150.
    • (2010) J.Biol. Chem. , vol.285 , pp. 32141-32150
    • Zhao, N.1    Gao, J.2    Enns, C.A.3    Knutson, M.D.4


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