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Volumn 16, Issue 10, 2012, Pages 1100-1108

The endoplasmic reticulum as the extracellular space inside the cell: Role in protein folding and glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; CALCIUM; CALCIUM BINDING PROTEIN; CALRETICULIN; CHAPERONE; DEHYDROASCORBIC ACID; GLUCOSE TRANSPORTER; GLUTATHIONE; PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 84859257455     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2011.4227     Document Type: Review
Times cited : (38)

References (59)
  • 2
    • 0035133393 scopus 로고    scopus 로고
    • ER calcium and the functions of intracellular organelles
    • DOI 10.1006/scdb.2000.0212
    • Ashby MC and Tepikin AV. ER calcium and the functions of intracellular organelles. Semin Cell Dev Biol 12: 11-17, 2001. (Pubitemid 32147101)
    • (2001) Seminars in Cell and Developmental Biology , vol.12 , Issue.1 , pp. 11-17
    • Ashby, M.C.1    Tepikin, A.V.2
  • 3
    • 0025788270 scopus 로고
    • 2+ binding domains
    • Baksh S and Michalak M. Expression of calreticulin in Es-cherichia coli and identification of its Ca2 + binding domains. J Biol Chem 266: 21458-21465, 1991. (Pubitemid 121000207)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.32 , pp. 21458-21465
    • Baksh, S.1    Michalak, M.2
  • 7
    • 1242294484 scopus 로고    scopus 로고
    • A Major Fraction of Endoplasmic Reticulum-located Glutathione Is Present as Mixed Disulfides with Protein
    • DOI 10.1074/jbc.M304951200
    • Bass R, Ruddock LW, Klappa P, and Freedman RB. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 279: 5257-5262, 2004. (Pubitemid 38220545)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5257-5262
    • Bass, R.1    Ruddock, L.W.2    Klappa, P.3    Freedman, R.B.4
  • 9
    • 77955663100 scopus 로고
    • The evolution of protein targeting and translocation systems
    • Bohnsack MT and Schleiff E. The evolution of protein targeting and translocation systems. Biochim Biophys Acta 1803: 1115-1130, 2010.
    • (1803) Biochim Biophys Acta , pp. 1115-1130
    • Bohnsack, M.T.1    Schleiff, E.2
  • 10
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the Mammalian endoplasmic reticulum
    • Braakman I and Bulleid NJ. Protein folding and modification in the Mammalian endoplasmic reticulum. Annu Rev Bio-chem 80: 71-99, 2011.
    • (2011) Annu Rev Bio-chem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 11
    • 33750340637 scopus 로고    scopus 로고
    • Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum
    • DOI 10.1021/bi0614378
    • Brockmeier A and Williams DB. Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum. Biochemistry 45: 12906-12916, 2006. (Pubitemid 44630877)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12906-12916
    • Brockmeier, A.1    Williams, D.B.2
  • 12
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of en-doplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell SR, Hill KJ, and Cooper AA. Degradation of en-doplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem 276: 23296-23303, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 13
    • 77149136381 scopus 로고    scopus 로고
    • Calcium binding chaperones of the endoplasmic reticulum
    • Coe H and Michalak M. Calcium binding chaperones of the endoplasmic reticulum. Gen Physiol Biophys 28: F96-F103, 2009.
    • (2009) Gen Physiol Biophys , vol.28
    • Coe, H.1    Michalak, M.2
  • 15
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • DOI 10.1016/0092-8674(94)90424-3
    • Crowley KS, Liao S, Worrell VE, Reinhart GD, and Johnson AE. Secretory proteins move through the endoplasmic re-ticulum membrane via an aqueous, gated pore. Cell 78: 461-471, 1994. (Pubitemid 24250810)
    • (1994) Cell , vol.78 , Issue.3 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 16
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo JW and Kaiser CA. Competition between glutathi-one and protein thiols for disulphide-bond formation. Nat Cell Biol 1: 130-135, 1999. (Pubitemid 129656016)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 17
    • 33645980003 scopus 로고    scopus 로고
    • Endoplasmic retic-ulum: A metabolic compartment
    • Csala M, Banhegyi G, and Benedetti A. Endoplasmic retic-ulum: A metabolic compartment. FEBS Lett 580: 2160-2165, 2006.
    • (2006) FEBS Lett , vol.580 , pp. 2160-2165
    • Csala, M.1    Banhegyi, G.2    Benedetti, A.3
  • 18
    • 0032755276 scopus 로고    scopus 로고
    • Ascorbate-mediated electron transfer in protein thiol oxidation in the endoplasmic reticulum
    • DOI 10.1016/S0014-5793(99)01412-X, PII S001457939901412X
    • Csala M, Braun L, Mile V, Kardon T, Szarka A, Kupcsulik P, Mandl J, and Banhegyi G. Ascorbate-mediated electron transfer in protein thiol oxidation in the endoplasmic retic-ulum. FEBS Lett 460: 539-543, 1999. (Pubitemid 29518434)
    • (1999) FEBS Letters , vol.460 , Issue.3 , pp. 539-543
    • Csala, M.1    Braun, L.2    Mile, V.3    Kardon, T.4    Szarka, A.5    Kupcsulik, P.6    Mandl, J.7    Banhegyi, G.8
  • 22
    • 0020318561 scopus 로고
    • Secretion of newly taken-up ascorbic acid by adrenomedullary chromaffin cells
    • Daniels AJ, Dean G, Viveros OH, and Diliberto EJ, Jr. Secretion of newly taken-up ascorbic acid by adrenomedullary chromaffin cells. Science 216: 737-739, 1982. (Pubitemid 12041773)
    • (1982) Science , vol.216 , Issue.4547 , pp. 737-739
    • Daniels, A.J.1    Dean, G.2    Viveros, O.H.3    Diliberto Jr., E.J.4
  • 24
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill DJ, Chia J, Senewiratne J, and Bard F. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J Cell Biol 189: 843-858, 2010.
    • (2010) J Cell Biol , vol.189 , pp. 843-858
    • Gill, D.J.1    Chia, J.2    Senewiratne, J.3    Bard, F.4
  • 25
    • 33750902737 scopus 로고    scopus 로고
    • The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control
    • DOI 10.1089/ars.2006.8.1391
    • Gorlach A, Klappa P, and Kietzmann T. The endoplasmic reticulum: folding, calcium homeostasis, signaling, and re-dox control. Antioxid Redox Signal 8: 1391-1418, 2006. (Pubitemid 44726319)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.9-10 , pp. 1391-1418
    • Gorlach, A.1    Klappa, P.2    Kietzmann, T.3
  • 27
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore thorough the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman BD, Chen JC, Johnson EE, and Johnson AE. The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell 89: 535-544, 1997. (Pubitemid 27511764)
    • (1997) Cell , vol.89 , Issue.4 , pp. 535-544
    • Hamman, B.D.1    Chen, J.-C.2    Johnson, E.E.3    Johnson, A.E.4
  • 28
    • 35549006797 scopus 로고    scopus 로고
    • 2+ Signaling and Cell Survival
    • DOI 10.1016/j.cell.2007.08.036, PII S0092867407010999
    • Hayashi T and Su TP. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 131: 596-610, 2007. (Pubitemid 350017760)
    • (2007) Cell , vol.131 , Issue.3 , pp. 596-610
    • Hayashi, T.1    Su, T.-P.2
  • 30
    • 0036423024 scopus 로고    scopus 로고
    • Transmembrane movement of dolichol linked carbohydrates during N-glycoprotein biosynthesis in the endoplasmic reticulum
    • DOI 10.1016/S1084-9521(02)00045-9
    • Helenius J and Aebi M. Transmembrane movement of do-lichol linked carbohydrates during N-glycoprotein biosynthesis in the endoplasmic reticulum. Semin Cell Dev Biol 13: 171-178, 2002. (Pubitemid 35304520)
    • (2002) Seminars in Cell and Developmental Biology , vol.13 , Issue.3 , pp. 171-178
    • Helenius, J.1    Aebi, M.2
  • 31
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 32
    • 1242317639 scopus 로고    scopus 로고
    • Molecular physiology and pathology of the nucleotide sugar transporter family (SLC35)
    • DOI 10.1007/s00424-003-1093-0, The ABCs of Solute Carriers: Physiological, Pathological and Therapeutic Implications of Human Membrane Transport Proteins
    • Ishida N and Kawakita M. Molecular physiology and pathology of the nucleotide sugar transporter family (SLC35). Pflugers Arch 447: 768-775, 2004. (Pubitemid 38241465)
    • (2004) Pflugers Archiv European Journal of Physiology , vol.447 , Issue.5 , pp. 768-775
    • Ishida, N.1    Kawakita, M.2
  • 35
    • 64549156522 scopus 로고    scopus 로고
    • Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum
    • Karala AR, Lappi AK, Saaranen MJ, and Ruddock LW. Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum. Antioxid Redox Signal 11: 963-970, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 963-970
    • Karala, A.R.1    Lappi, A.K.2    Saaranen, M.J.3    Ruddock, L.W.4
  • 36
    • 0024325535 scopus 로고
    • Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
    • Kassenbrock CK and Kelly RB. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J 8: 1461-1467, 1989. (Pubitemid 19274372)
    • (1989) EMBO Journal , vol.8 , Issue.5 , pp. 1461-1467
    • Kassenbrock, C.K.1    Kelly, R.B.2
  • 37
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman RJ. Stress signaling from the lumen of the endo-plasmic reticulum: Coordination of gene transcriptional and translational controls. Genes Dev 13: 1211-1233, 1999. (Pubitemid 29250189)
    • (1999) Genes and Development , vol.13 , Issue.10 , pp. 1211-1233
    • Kaufman, R.J.1
  • 38
    • 79955878526 scopus 로고    scopus 로고
    • Reexamination of the role of interplay between glutathione and protein disulfide isom-erase
    • Lappi AK and Ruddock LW. Reexamination of the role of interplay between glutathione and protein disulfide isom-erase. J Mol Biol 409: 238-249, 2011.
    • (2011) J Mol Biol , vol.409 , pp. 238-249
    • Lappi, A.K.1    Ruddock, L.W.2
  • 39
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins
    • DOI 10.1016/j.tibs.2005.04.010, PII S0968000405001180, Celebrating 50 Years of the IUBMB
    • Lederkremer GZ and Glickman MH. A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci 30: 297-303, 2005. (Pubitemid 40799047)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.6 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 40
    • 1842405433 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1074/jbc.272.49.30873
    • Lievremont JP, Rizzuto R, Hendershot L, and Meldolesi J. BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+. J Biol Chem 272: 30873-30879, 1997. (Pubitemid 27527530)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30873-30879
    • Lievremont, J.-P.1    Rizzuto, R.2    Hendershot, L.3    Meldolesi, J.4
  • 41
    • 40049100372 scopus 로고    scopus 로고
    • The translocon and the non-specific transport of small molecules in the endoplasmic reticulum (Review)
    • DOI 10.1080/09687680701670481, PII 784706774
    • Lizak B, Csala M, Benedetti A, and Banhegyi G. The trans-locon and the non-specific transport of small molecules in the endoplasmic reticulum (Review). Mol Membr Biol 25: 95-101, 2008. (Pubitemid 351320500)
    • (2008) Molecular Membrane Biology , vol.25 , Issue.2 , pp. 95-101
    • Lizak, B.1    Csala, M.2    Benedetti, A.3    Banhegyi, G.4
  • 42
    • 67949124778 scopus 로고    scopus 로고
    • Translocation of proteins through the Sec61 and SecYEG channels
    • Mandon EC, Trueman SF, and Gilmore R. Translocation of proteins through the Sec61 and SecYEG channels. Curr Opin Cell Biol 21: 501-507, 2009.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 501-507
    • Mandon, E.C.1    Trueman, S.F.2    Gilmore, R.3
  • 43
    • 33751017659 scopus 로고    scopus 로고
    • Family 47 alpha-mannosidases in N-glycan processing
    • Mast SW and Moremen KW. Family 47 alpha-mannosidases in N-glycan processing. Methods Enzymol 415: 31-46, 2006.
    • (2006) Methods Enzymol , vol.415 , pp. 31-46
    • Mast, S.W.1    Moremen, K.W.2
  • 44
    • 0031594742 scopus 로고    scopus 로고
    • 2+ store: A view from the lumen
    • DOI 10.1016/S0968-0004(97)01143-2, PII S0968000497011432
    • Meldolesi J and Pozzan T. The endoplasmic reticulum Ca2 + store: A view from the lumen. Trends Biochem Sci 23: 10-14, 1998. (Pubitemid 28093986)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.1 , pp. 10-14
    • Meldolesi, J.1    Pozzan, T.2
  • 45
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • DOI 10.1016/S0143416002001884
    • Michalak M, Robert Parker JM, and Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticu-lum. Cell Calcium 32: 269-278, 2002. (Pubitemid 36175750)
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 269-278
    • Michalak, M.1    Parker, J.M.R.2    Opas, M.3
  • 47
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllyla R, Majamaa K, Gunzler V, Hanauske-Abel HM, and Kivirikko KI. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxy-lase and lysyl hydroxylase. J Biol Chem 259: 5403-5405, 1984. (Pubitemid 14144988)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.9 , pp. 5403-5405
    • Myllyla, R.1    Majamaa, K.2    Gunzler, V.3
  • 49
    • 80051686315 scopus 로고    scopus 로고
    • Golgi localization of ER-ManI defines spatial separation of the mammalian glyco-protein quality control system
    • Pan S, Wang S, Utama B, Huang L, Blok N, Estes MK, Moremen KW, and Sifers RN. Golgi localization of ER-ManI defines spatial separation of the mammalian glyco-protein quality control system. Mol Biol Cell 22: 2810-2822, 2011.
    • (2011) Mol Biol Cell , vol.22 , pp. 2810-2822
    • Pan, S.1    Wang, S.2    Utama, B.3    Huang, L.4    Blok, N.5    Estes, M.K.6    Moremen, K.W.7    Sifers, R.N.8
  • 51
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, and Williams DB. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J 18: 6718-6729, 1999.
    • (1999) EMBO J , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 52
    • 1842561598 scopus 로고    scopus 로고
    • The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells
    • DOI 10.1083/jcb.200312079
    • Snapp EL, Reinhart GA, Bogert BA, Lippincott-Schwartz J, and Hegde RS. The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells. J Cell Biol 164: 997-1007, 2004. (Pubitemid 38429126)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 997-1007
    • Snapp, E.L.1    Reinhart, G.A.2    Bogert, B.A.3    Lippincott-Schwartz, J.4    Hegde, R.S.5
  • 54
    • 0036862532 scopus 로고    scopus 로고
    • 2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • DOI 10.1016/S1097-2765(02)00696-2
    • Tu BP and Weissman JS. The FAD-and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell 10: 983-994, 2002. (Pubitemid 35453820)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 55
    • 0023045540 scopus 로고
    • Dolichyl phosphate induces non-bilayer structures, vesicle fusion and transbilayer movement of lipids: A model membrane study
    • van Duijn G, Valtersson C, Chojnacki T, Verkleij AJ, Dallner G, and de Kruijff B. Dolichyl phosphate induces non-bilayer structures, vesicle fusion and transbilayer movement of lipids: A model membrane study. Biochim Biophys Acta 861: 211-223, 1986.
    • (1986) Biochim Biophys Acta , vol.861 , pp. 211-223
    • Van Duijn, G.1    Valtersson, C.2    Chojnacki, T.3    Verkleij, A.J.4    Dallner, G.5    De Kruijff, B.6
  • 56
    • 0037086660 scopus 로고    scopus 로고
    • The glucose-6-phosphatase system
    • DOI 10.1042/0264-6021:3620513
    • van Schaftingen E and Gerin I. The glucose-6-phosphatase system. Biochem J 362: 513-532, 2002. (Pubitemid 34242301)
    • (2002) Biochemical Journal , vol.362 , Issue.3 , pp. 513-532
    • Van Schaftingen, E.1    Gerin, I.2
  • 59
    • 79953171866 scopus 로고    scopus 로고
    • Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments
    • Wijeyesakere SJ, Gafni AA, and Raghavan M. Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments. J Biol Chem 286: 8771-8785, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 8771-8785
    • Wijeyesakere, S.J.1    Gafni, A.A.2    Raghavan, M.3


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