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Volumn 164, Issue 1, 2004, Pages 35-46

Ca2+-dependent redox modulation of SERCA 2b by ERp57

Author keywords

Calcium ATPases; Calcium oscillations; Calreticulin; Endoplasmic reticulum; Glycoprotein folding

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; CALRETICULIN; OXIDOREDUCTASE; PROTEIN ERP57; SARCOENDOPLASMIC RETICULUM ADENOSINE TRIPHOSPHATASE 2B; UNCLASSIFIED DRUG; CALCIUM; CYSTEINE; GRP58 PROTEIN, RAT; HEAT SHOCK PROTEIN; ISOMERASE; ISOPROTEIN; PDIA3 PROTEIN, HUMAN; PROTEIN DISULFIDE ISOMERASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; THIOL DERIVATIVE;

EID: 0347753252     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200307010     Document Type: Article
Times cited : (213)

References (61)
  • 1
    • 0038080954 scopus 로고    scopus 로고
    • Multiple effects of SERCA2b mutations associated with Darier's disease
    • Ahn, W., M.G. Lee, K.H. Kim, and S. Muallem. 2003. Multiple effects of SERCA2b mutations associated with Darier's disease. J. Biol. Chem. 278:20795-20801.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20795-20801
    • Ahn, W.1    Lee, M.G.2    Kim, K.H.3    Muallem, S.4
  • 2
    • 0037013950 scopus 로고    scopus 로고
    • The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
    • Antoniou, A.N., S. Ford, M. Alphey, A. Osborne, T. Elliott, and S.J. Powis. 2002. The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J. 21:2655-2663.
    • (2002) EMBO J. , vol.21 , pp. 2655-2663
    • Antoniou, A.N.1    Ford, S.2    Alphey, M.3    Osborne, A.4    Elliott, T.5    Powis, S.J.6
  • 3
    • 0035133393 scopus 로고    scopus 로고
    • ER calcium and the functions of intracellular organelles
    • Ashby, M.C., and A.V. Tepikin. 2001. ER calcium and the functions of intracellular organelles. Semin. Cell Dev. Biol. 12:11-17.
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 11-17
    • Ashby, M.C.1    Tepikin, A.V.2
  • 4
    • 0034001185 scopus 로고    scopus 로고
    • 2+-pump isoform SERCA3a is more resistant to superoxide damage than SERCA2b
    • 2+-pump isoform SERCA3a is more resistant to superoxide damage than SERCA2b. Mol. Cell. Biochem. 203:17-21.
    • (2000) Mol. Cell. Biochem. , vol.203 , pp. 17-21
    • Barnes, K.A.1    Samson, S.E.2    Grover, A.K.3
  • 5
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle, D., D. Weeks, and G. Sachs. 1995. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J. Biol. Chem. 270:25678-25684.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 7
    • 0032531818 scopus 로고    scopus 로고
    • Calcium - A life and death signal
    • Berridge, M.J., M.D. Bootman, and P. Lipp. 1998. Calcium - a life and death signal. Nature. 395:645-648.
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 8
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Y. Zhang, L.M. Hendershot, H.P. Harding, and D. Ron. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:326-332.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 9
    • 0037225830 scopus 로고    scopus 로고
    • Accessory proteins and the assembly of human class I MHC molecules: A molecular and structural perspective
    • Bouvier, M. 2003. Accessory proteins and the assembly of human class I MHC molecules: a molecular and structural perspective. Mol. Immunol. 39:697-706.
    • (2003) Mol. Immunol. , vol.39 , pp. 697-706
    • Bouvier, M.1
  • 10
    • 0027231872 scopus 로고
    • Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase
    • Camacho, P., and J.D. Lechleiter. 1993. Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase. Science. 260:226-229.
    • (1993) Science , vol.260 , pp. 226-229
    • Camacho, P.1    Lechleiter, J.D.2
  • 12
    • 0003981344 scopus 로고    scopus 로고
    • Xenopus oocytes as a tool in calcium signaling research
    • J.W. Putney, Jr., editor. CRC Press, Boca Raton, FL
    • Camacho, P., and J.D. Lechleiter. 2000. Xenopus oocytes as a tool in calcium signaling research. In Calcium Signaling. J.W. Putney, Jr., editor. CRC Press, Boca Raton, FL. 157-182.
    • (2000) Calcium Signaling , pp. 157-182
    • Camacho, P.1    Lechleiter, J.D.2
  • 13
    • 14444280363 scopus 로고    scopus 로고
    • Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum
    • Chen, L.B., S.K. Nigam, and G. Kuznetsov. 1997. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J. Biol. Chem. 272:3057-3063.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3057-3063
    • Chen, L.B.1    Nigam, S.K.2    Kuznetsov, G.3
  • 14
    • 0038457818 scopus 로고    scopus 로고
    • The thioredoxin-like fold: Hidden domains in protein disulfide isomerases and other chaperone proteins
    • Clissold, P.M., and R. Bicknell. 2003. The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins. Bioessays. 25:603-611.
    • (2003) Bioessays , vol.25 , pp. 603-611
    • Clissold, P.M.1    Bicknell, R.2
  • 16
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick, T.P., N. Bangia, D.R. Peaper, and P. Cresswell. 2002. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity. 16:87-98.
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 18
    • 0030791385 scopus 로고    scopus 로고
    • published erratum
    • 2+ response amplitude and duration. Nature. 386:855-858. (published erratum in Nature. 1997. 388:308)
    • (1997) Nature , vol.388 , pp. 308
  • 19
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and A. Helenius. 2003. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4:181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 22
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A., and F. Fabiato. 1979. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. (Paris). 75:463-505.
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 24
    • 0036198797 scopus 로고    scopus 로고
    • Protein disulfide isomerases exploit synergy between catalytic and specific binding domains
    • Freedman, R.B., P. Klappa, and L.W. Ruddock. 2002. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains. EMBO Rep. 3:136-140.
    • (2002) EMBO Rep. , vol.3 , pp. 136-140
    • Freedman, R.B.1    Klappa, P.2    Ruddock, L.W.3
  • 28
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding, H.P., M. Calfon, F. Urano, I. Novoa, and D. Ron. 2002. Transcriptional and translational control in the mammalian unfolded protein response. Annu. Rev. Cell Dev. Biol. 18:575-599.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 29
    • 0030066103 scopus 로고    scopus 로고
    • Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3)
    • Hardman, K.D., and D.R. Wetmore. 1996. Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3). Biochemistry. 35:6549-6558.
    • (1996) Biochemistry , vol.35 , pp. 6549-6558
    • Hardman, K.D.1    Wetmore, D.R.2
  • 30
    • 0034733916 scopus 로고    scopus 로고
    • Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?
    • High, S., F.J. Lecomte, S.J. Russell, B.M. Abell, and J.D. Oliver. 2000. Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones? FEBS Lett. 476:38-41.
    • (2000) FEBS Lett. , vol.476 , pp. 38-41
    • High, S.1    Lecomte, F.J.2    Russell, S.J.3    Abell, B.M.4    Oliver, J.D.5
  • 31
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano, N., F. Shibasaki, R. Sakai, T. Tanaka, J. Nishida, Y. Yazaki, T. Takenawa, and H. Hirai. 1995. Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur. J. Biochem. 234:336-342.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1    Shibasaki, F.2    Sakai, R.3    Tanaka, T.4    Nishida, J.5    Yazaki, Y.6    Takenawa, T.7    Hirai, H.8
  • 32
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. 1979. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254:9627-9632.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 33
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes, E.A., and P. Cresswell. 1998. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 8:709-712.
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 34
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., A.J. Sinskey, and H.F. Lodish. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 35
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John, L.M., J.D. Lechleiter, and P. Camacho. 1998. Differential modulation of SERCA2 isoforms by calreticulin. J. Cell Biol. 142:963-973.
    • (1998) J. Cell Biol. , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 36
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R.J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1211-1233.
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 37
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova, Z., and D.H. Wolf. 2003. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22:2309-2317.
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 38
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin. ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach, M.R., M.F. Cohen-Doyle, D.Y. Thomas, and D.B. Williams. 2002. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 277:29686-29697.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 39
    • 0032580157 scopus 로고    scopus 로고
    • Cell-permeant caged InsP3 ester shows that Ca21 spike frequency can optimize gene expression
    • Li W., J. Llopis, M. Whitney, G. Zlokarnik, and R.Y. Tsien. 1998. Cell-permeant caged InsP3 ester shows that Ca21 spike frequency can optimize gene expression. Nature. 392:936-941.
    • (1998) Nature , vol.392 , pp. 936-941
    • Li, W.1    Llopis, J.2    Whitney, M.3    Zlokarnik, G.4    Tsien, R.Y.5
  • 40
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist, J.A., O.N. Jensen, M. Mann, and G.J. Hammerling. 1998. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17:2186-2195.
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 41
    • 0242649039 scopus 로고    scopus 로고
    • Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family
    • Marcus, N., D. Shaffer, P. Farrar, and M. Green. 1996. Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family. Biochim. Biophys. Acta. 1309:253-260.
    • (1996) Biochim. Biophys. Acta , vol.1309 , pp. 253-260
    • Marcus, N.1    Shaffer, D.2    Farrar, P.3    Green, M.4
  • 43
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice, N.A., and S.J. Powis. 1998. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol. 8:713-716.
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 44
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J.D., F.J. van der Wal, N.J. Bulleid, and S. High. 1997. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science. 275:86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 45
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver, J.D., H.L. Roderick, D.H. Llewellyn, and S. High. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell. 10:2573-2582.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 46
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil, C., and P. Walter. 2001. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13:349-355.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 47
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan, T., R. Rizzuto, P. Volpe, and J. Meldolesi. 1994. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74:595-636.
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 50
    • 0032877634 scopus 로고    scopus 로고
    • ATP2A2 mutations in Darier's disease: Variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class
    • Ruiz-Perez, V.L., S.A. Carter, E. Healy, C. Todd, J.L. Rees, P.M. Steijlen, A.J. Carmichael, H.M. Lewis, D. Hohl, P. Itin, et al. 1999. ATP2A2 mutations in Darier's disease: variant cutaneous phenotypes are associated with missense mutations, but neuropsychiatric features are independent of mutation class. Hum. Mol. Genet. 8:1621-1630.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1621-1630
    • Ruiz-Perez, V.L.1    Carter, S.A.2    Healy, E.3    Todd, C.4    Rees, J.L.5    Steijlen, P.M.6    Carmichael, A.J.7    Lewis, H.M.8    Hohl, D.9    Itin, P.10
  • 52
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J.D., J.J. Bergeron, Y. Li, S. Borisova, M. Hahn, D.Y. Thomas, and M. Cygler. 2001. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell. 8:633-644.
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 55
    • 0035844120 scopus 로고    scopus 로고
    • Classes of thiols that influence the activity of the skeletal muscle calcium release channel
    • Sun, J., L. Xu, J.P. Eu, J.S. Stamler, and G. Meissner. 2001. Classes of thiols that influence the activity of the skeletal muscle calcium release channel. J. Biol. Chem. 276:15625-15630.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15625-15630
    • Sun, J.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 56
    • 0032529113 scopus 로고    scopus 로고
    • The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming
    • Van der Wal, F.J., J.D. Oliver, and S. High. 1998. The transient association of ERp57 with N-glycosylated proteins is regulated by glucose trimming. Eur. J. Biochem. 256:51-59.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 51-59
    • Van Der Wal, F.J.1    Oliver, J.D.2    High, S.3
  • 57
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos, A., M. Michalak, M.A. Lehrman, and D.B. Williams. 1998. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry. 37:3480-3490.
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 58
    • 0032780022 scopus 로고    scopus 로고
    • The cellular response to protein misfolding in the endoplasmic reticulum
    • Welihinda, A.A., W. Tirasophon, and R.J. Kaufman. 1999. The cellular response to protein misfolding in the endoplasmic reticulum. Gene Expr. 7:293-300.
    • (1999) Gene Expr. , vol.7 , pp. 293-300
    • Welihinda, A.A.1    Tirasophon, W.2    Kaufman, R.J.3
  • 59
    • 0034711213 scopus 로고    scopus 로고
    • Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators
    • Xia, R., T. Stangler, and J.J. Abramson. 2000. Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators. J. Biol. Chem. 275:36556-36561.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36556-36561
    • Xia, R.1    Stangler, T.2    Abramson, J.J.3
  • 61
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun, A., N.J. Darby, D.C. Tessier, M. Michalak, J.J. Bergeron, and D.Y. Thomas. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273:6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.5    Thomas, D.Y.6


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