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Volumn 20, Issue 8, 2015, Pages 13689-13704

Glycoprotein quality control and endoplasmic reticulum stress

Author keywords

Calnexin; Calreticulin; Chaperone; Endoplasmic reticulum; Stress

Indexed keywords

GLYCOPROTEIN;

EID: 84941249224     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules200813689     Document Type: Review
Times cited : (66)

References (112)
  • 1
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert, D.N.; Molinari, M. In and out of the ER: Protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 2007, 87, 1377-1408.
    • (2007) Physiol. Rev. , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 2
    • 0034235397 scopus 로고    scopus 로고
    • Calcium, a signaling molecule in the endoplasmic reticulum?
    • Corbett, E.F.; Michalak, M. Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem. Sci. 2000, 25, 307-311.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 307-311
    • Corbett, E.F.1    Michalak, M.2
  • 4
    • 0036878801 scopus 로고    scopus 로고
    • The endoplasmic reticulum and neuronal calcium signalling
    • Verkhratsky, A. The endoplasmic reticulum and neuronal calcium signalling. Cell Calcium 2002, 32, 393-404.
    • (2002) Cell Calcium , vol.32 , pp. 393-404
    • Verkhratsky, A.1
  • 6
    • 84873684054 scopus 로고    scopus 로고
    • Coping with endoplasmic reticulum stress in the cardiovascular system
    • Groenendyk, J.; Agellon, L.B.; Michalak, M. Coping with endoplasmic reticulum stress in the cardiovascular system. Annu. Rev. Physiol. 2013, 75, 49-67.
    • (2013) Annu. Rev. Physiol. , vol.75 , pp. 49-67
    • Groenendyk, J.1    Agellon, L.B.2    Michalak, M.3
  • 8
    • 48249088868 scopus 로고    scopus 로고
    • Distinct flippases translocate glycerophospholipids and oligosaccharide diphosphate dolichols across the endoplasmic reticulum
    • Sanyal, S.; Frank, C.G.; Menon, A.K. Distinct flippases translocate glycerophospholipids and oligosaccharide diphosphate dolichols across the endoplasmic reticulum. Biochemistry 2008, 47, 7937-7946.
    • (2008) Biochemistry , vol.47 , pp. 7937-7946
    • Sanyal, S.1    Frank, C.G.2    Menon, A.K.3
  • 10
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F.; Gnad, F.; Wisniewski, J.R.; Mann, M. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell 2010, 141, 897-907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 11
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus
    • Nilsson, T.; Warren, G. Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell. Biol. 1994, 6, 517-521.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 13
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation
    • Mohorko, E.; Glockshuber, R.; Aebi, M. Oligosaccharyltransferase: The central enzyme of N-linked protein glycosylation. J. Inherit. Metab. Dis. 2011, 34, 869-878.
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 15
    • 22544467505 scopus 로고    scopus 로고
    • More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle
    • Deprez, P.; Gautschi, M.; Helenius, A. More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle. Mol. Cell. 2005, 19, 183-195.
    • (2005) Mol. Cell. , vol.19 , pp. 183-195
    • Deprez, P.1    Gautschi, M.2    Helenius, A.3
  • 16
    • 84867316962 scopus 로고    scopus 로고
    • An MBoC favorite: Malectin: A novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation
    • Hebert, D.N. An MBoC favorite: Malectin: A novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol. Biol. Cell. 2012, 23, 2236-2236.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 2236-2236
    • Hebert, D.N.1
  • 17
    • 33751508817 scopus 로고    scopus 로고
    • N-glycan processing in ER quality control
    • Ruddock, L.W.; Molinari, M. N-glycan processing in ER quality control. J. Cell. Sci. 2006, 119, 4373-4380.
    • (2006) J. Cell. Sci. , vol.119 , pp. 4373-4380
    • Ruddock, L.W.1    Molinari, M.2
  • 18
    • 0026077745 scopus 로고
    • Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain
    • Shailubhai, K.; Pukazhenthi, B.S.; Saxena, E.S.; Varma, G.M.; Vijay, I.K. Glucosidase I, a transmembrane endoplasmic reticular glycoprotein with a luminal catalytic domain. J. Biol. Chem. 1991, 266, 16587-16593.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16587-16593
    • Shailubhai, K.1    Pukazhenthi, B.S.2    Saxena, E.S.3    Varma, G.M.4    Vijay, I.K.5
  • 19
    • 54249136020 scopus 로고    scopus 로고
    • Malectin: A novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation
    • Schallus, T.; Jaeckh, C.; Feher, K.; Palma, A.S.; Liu, Y.; Simpson, J.C.; Mackeen, M.; Stier, G.; Gibson, T.J.; Feizi, T.; et al. Malectin: A novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol. Biol. Cell. 2008, 19, 3404-3414.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 3404-3414
    • Schallus, T.1    Jaeckh, C.2    Feher, K.3    Palma, A.S.4    Liu, Y.5    Simpson, J.C.6    Mackeen, M.7    Stier, G.8    Gibson, T.J.9    Feizi, T.10
  • 21
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware, F.E.; Vassilakos, A.; Peterson, P.A.; Jackson, M.R.; Lehrman, M.A.; Williams, D.B. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 1995, 270, 4697-4704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697-4704
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 22
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro, R.G.; Zhu, Q.; Bhoyroo, V.; Söling, H.D. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 1996, 271, 11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.D.4
  • 23
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
    • Trombetta, E.S.; Simons, J.F.; Helenius, A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 1996, 271, 27509-27516.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 24
    • 70249110040 scopus 로고    scopus 로고
    • Sugar-binding activity of the MRH domain in the ERα-glucosidase II β subunit is important for efficient glucose trimming
    • Hu, D.; Kamiya, Y.; Totani, K.; Kamiya, D.; Kawasaki, N.; Yamaguchi, D.; Matsuo, I.; Matsumoto, N.; Ito, Y.; Kato, K.; et al. Sugar-binding activity of the MRH domain in the ERα-glucosidase II β subunit is important for efficient glucose trimming. Glycobiology 2009, 19, 1127-1135.
    • (2009) Glycobiology , vol.19 , pp. 1127-1135
    • Hu, D.1    Kamiya, Y.2    Totani, K.3    Kamiya, D.4    Kawasaki, N.5    Yamaguchi, D.6    Matsuo, I.7    Matsumoto, N.8    Ito, Y.9    Kato, K.10
  • 25
    • 84878756888 scopus 로고    scopus 로고
    • Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum
    • Olson, L.J.; Orsi, R.; Alculumbre, S.G.; Peterson, F.C.; Stigliano, I.D.; Parodi, A.J.; D'Alessio, C.; Dahms, N.M. Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum. J. Biol. Chem. 2013, 288, 16460-16475.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16460-16475
    • Olson, L.J.1    Orsi, R.2    Alculumbre, S.G.3    Peterson, F.C.4    Stigliano, I.D.5    Parodi, A.J.6    D'Alessio, C.7    Dahms, N.M.8
  • 30
    • 84881535343 scopus 로고    scopus 로고
    • Calnexin controls the STAT3-mediated transcriptional response to EGF
    • Lakkaraju, A.K.; van der Goot, F.G. Calnexin Controls the STAT3-Mediated Transcriptional Response to EGF. Mol. Cell 2013, 51, 386-396.
    • (2013) Mol. Cell , vol.51 , pp. 386-396
    • Lakkaraju, A.K.1    Van Der Goot, F.G.2
  • 31
    • 77952583799 scopus 로고    scopus 로고
    • Calnexin phosphorylation: Linking cytoplasmic signalling to endoplasmic reticulum lumenal functions
    • Chevet, E.; Smirle, J.; Cameron, P.H.; Thomas, D.Y.; Bergeron, J.J. Calnexin phosphorylation: Linking cytoplasmic signalling to endoplasmic reticulum lumenal functions. Semin. Cell Dev. Biol. 2010, 21, 486-490.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 486-490
    • Chevet, E.1    Smirle, J.2    Cameron, P.H.3    Thomas, D.Y.4    Bergeron, J.J.5
  • 32
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak, M.; Groenendyk, J.; Szabo, E.; Gold, L.I.; Opas, M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 2009, 417, 651-666.
    • (2009) Biochem. J. , vol.417 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 33
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D.N.; Foellmer, B.; Helenius, A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 1995, 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 34
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta, E.S.; Parodi, A.J. Quality Control and Protein Folding in the Secretory Pathway. Annu. Rev. Cell Dev. Biol. 2003, 649-676.
    • (2003) Annu. Rev. Cell Dev. Biol. , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 35
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • Hebert, D.N.; Garman, S.C.; Molinari, M. The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 2005, 15, 364-370.
    • (2005) Trends Cell Biol. , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 36
    • 84922143124 scopus 로고    scopus 로고
    • Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: Crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase
    • Zhu, T.; Satoh, T.; Kato, K. Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: Crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase. Sci. Rep. 2014, 4, doi:10.1038/srep07322.
    • (2014) Sci. Rep. , vol.4
    • Zhu, T.1    Satoh, T.2    Kato, K.3
  • 37
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M.; Parodi, A.J. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 1995, 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 38
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink, A.L. Chaperone-mediated protein folding. Physiol. Rev. 1999, 79, 425-449.
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 40
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams, D.B. Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci. 2006, 119, 615-623.
    • (2006) J. Cell Sci. , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 42
    • 0034799402 scopus 로고    scopus 로고
    • The Structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J.D.; Bergeron, J.J.; Li, Y.; Borisova, S.; Hahn, M.; Thomas, D.Y.; Cygler, M. The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 2001, 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
  • 44
    • 0029019816 scopus 로고
    • Enhanced expression of calreticulin in the nucleus of radioresistant squamous carcinoma cells in response to ionizing radiation
    • Ramsamooj, P.; Notario, V.; Dritschilo, A. Enhanced expression of calreticulin in the nucleus of radioresistant squamous carcinoma cells in response to ionizing radiation. Cancer Res. 1995, 55, 3016-3021.
    • (1995) Cancer Res. , vol.55 , pp. 3016-3021
    • Ramsamooj, P.1    Notario, V.2    Dritschilo, A.3
  • 45
    • 84912041938 scopus 로고    scopus 로고
    • Calreticulin is localized at mitochondria of rat cardiomyocytes and affected by furazolidone
    • Shan, H.; Wei, J.; Zhang, M.; Lin, L.; Yan, R.; Zhu, Y.; Zhang, R. Calreticulin is localized at mitochondria of rat cardiomyocytes and affected by furazolidone. Mol. Cell Biochem. 2014, 397, 125-130.
    • (2014) Mol. Cell Biochem. , vol.397 , pp. 125-130
    • Shan, H.1    Wei, J.2    Zhang, M.3    Lin, L.4    Yan, R.5    Zhu, Y.6    Zhang, R.7
  • 46
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • Afshar, N, Black, B.E.; Paschal, B.M. Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell. Biol. 2005, 25, 8844-8853.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 47
    • 0042170209 scopus 로고    scopus 로고
    • Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration
    • Orr, A.W.; Elzie, C.A.; Kucik, D.F.; Murphy-Ullrich, J.E. Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration. J. Cell Sci. 2003, 116, 2917-2927.
    • (2003) J. Cell Sci. , vol.116 , pp. 2917-2927
    • Orr, A.W.1    Elzie, C.A.2    Kucik, D.F.3    Murphy-Ullrich, J.E.4
  • 51
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach, M.R.; Cohen-Doyle, M.F.; Thomas, D.Y.; Williams, D.B. Localization of the Lectin, ERp57 Binding, and Polypeptide Binding Sites of Calnexin and Calreticulin. J. Biol. Chem. 2002, 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
  • 52
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • Kapoor, M.; Ellgaard, L.; Gopalakrishnapai, J.; Schirra, C.; Gemma, E.; Oscarson, S.; Helenius, A.; Surolia, A. Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 2004, 43, 97-106.
    • (2004) Biochemistry , vol.43 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3    Schirra, C.4    Gemma, E.5    Oscarson, S.6    Helenius, A.7    Surolia, A.8
  • 53
    • 26944462066 scopus 로고    scopus 로고
    • Delineation of the lectin site of the molecular chaperone calreticulin
    • Thomson, S.P.; Williams, D.B. Delineation of the lectin site of the molecular chaperone calreticulin. Cell Stress Chaperones 2005, 10, 242-251.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 242-251
    • Thomson, S.P.1    Williams, D.B.2
  • 55
    • 0037829617 scopus 로고    scopus 로고
    • Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong α1-antitrypsin by human ER mannosidase I
    • Hosokawa, N.; Tremblay, L.O.; You, Z.; Herscovics, A.; Wada, I.; Nagata, K. Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong α1-antitrypsin by human ER mannosidase I. J. Biol. Chem. 2003, 278, 26287-26294.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26287-26294
    • Hosokawa, N.1    Tremblay, L.O.2    You, Z.3    Herscovics, A.4    Wada, I.5    Nagata, K.6
  • 59
    • 84873027092 scopus 로고    scopus 로고
    • Compartmentalization of endoplasmic reticulum quality control and ER-associated degradation factors
    • Leitman, J.; Ron, E.; Ogen-Shtern, N.; Lederkremer, G.Z. Compartmentalization of endoplasmic reticulum quality control and ER-associated degradation factors. DNA Cell Biol. 2013, 32, 2-7.
    • (2013) DNA Cell Biol. , vol.32 , pp. 2-7
    • Leitman, J.1    Ron, E.2    Ogen-Shtern, N.3    Lederkremer, G.Z.4
  • 60
    • 84931571933 scopus 로고    scopus 로고
    • Glycan regulation of ER-associated degradation through compartmentalization
    • Benyair, R.; Ogen-Shtern, N.; Lederkremer, G.Z. Glycan regulation of ER-associated degradation through compartmentalization. Semin. Cell Dev. Biol. 2015, 41, 99-109.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 99-109
    • Benyair, R.1    Ogen-Shtern, N.2    Lederkremer, G.Z.3
  • 61
    • 38749122389 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation
    • Avezov, E.; Frenkel, Z.; Ehrlich, M.; Herscovics, A.; Lederkremer, G.Z. Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol. Biol. Cell 2008, 19, 216-225.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 216-225
    • Avezov, E.1    Frenkel, Z.2    Ehrlich, M.3    Herscovics, A.4    Lederkremer, G.Z.5
  • 62
    • 34548402513 scopus 로고    scopus 로고
    • Stimulation of ERAD of misfolded null Hong Kong α1-antitrypsin by Golgi α1,2-mannosidases
    • Hosokawa, N.; You, Z.; Tremblay, L.O.; Nagata, K.; Herscovics, A. Stimulation of ERAD of misfolded null Hong Kong α1-antitrypsin by Golgi α1,2-mannosidases. Biochem. Biophys. Res. Commun. 2007, 362, 626-632.
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 626-632
    • Hosokawa, N.1    You, Z.2    Tremblay, L.O.3    Nagata, K.4    Herscovics, A.5
  • 63
    • 84920946243 scopus 로고    scopus 로고
    • Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates
    • Benyair, R.; Ogen-Shtern, N.; Mazkereth, N.; Shai, B.; Ehrlich, M.; Lederkremer, G.Z. Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates. Mol. Biol. Cell 2015, 26, 172-184.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 172-184
    • Benyair, R.1    Ogen-Shtern, N.2    Mazkereth, N.3    Shai, B.4    Ehrlich, M.5    Lederkremer, G.Z.6
  • 64
    • 43549087339 scopus 로고    scopus 로고
    • Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
    • Cali, T.; Galli, C.; Olivari, S.; Molinari, M. Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities. Biochem. Biophys. Res. Commun. 2008, 371, 405-410.
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 405-410
    • Cali, T.1    Galli, C.2    Olivari, S.3    Molinari, M.4
  • 65
    • 34248356819 scopus 로고    scopus 로고
    • EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
    • Zuber, C.; Cormier, J.H.; Guhl, B.; Santimaria, R.; Hebert, D.N.; Roth, J. EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc. Natl. Acad. Sci. USA 2007, 104, 4407-4412.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4407-4412
    • Zuber, C.1    Cormier, J.H.2    Guhl, B.3    Santimaria, R.4    Hebert, D.N.5    Roth, J.6
  • 66
    • 0141706616 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2
    • Frenkel, Z.; Gregory, W.; Kornfeld, S.; Lederkremer, G.Z. Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2. J. Biol. Chem. 2003, 278, 34119-34124.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34119-34124
    • Frenkel, Z.1    Gregory, W.2    Kornfeld, S.3    Lederkremer, G.Z.4
  • 67
    • 84931565973 scopus 로고    scopus 로고
    • N-linked sugar-regulated protein folding and quality control in the ER
    • Tannous, A.; Pisoni, G.B.; Hebert, D.N.; Molinari, M. N-linked sugar-regulated protein folding and quality control in the ER. Semin. Cell Dev. Biol. 2015, 41, 79-89.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 79-89
    • Tannous, A.1    Pisoni, G.B.2    Hebert, D.N.3    Molinari, M.4
  • 69
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M.C.; Ferrero-Garcia, M.A.; Parodi, A.J. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 1992, 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 70
    • 79957596037 scopus 로고    scopus 로고
    • Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo
    • Stigliano, I.D.; Alculumbre, S.G.; Labriola, C.A.; Parodi, A.J.; D'Alessio, C. Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo. Mol. Biol. Cell 2011, 22, 1810-1823.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1810-1823
    • Stigliano, I.D.1    Alculumbre, S.G.2    Labriola, C.A.3    Parodi, A.J.4    D'Alessio, C.5
  • 71
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J.C.; Shaler, T.A.; Tyler, R.E.; Kopito, R.R. OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 2008, 10, 272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 73
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley, B.N.; Ploegh, H.L. Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA 2005, 102, 14296-14301.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 74
  • 75
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B.; Ye, Y.; Rapoport, T.A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 2002, 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 76
    • 41649116014 scopus 로고    scopus 로고
    • Derlin-1 facilitates the retro-translocation of cholera toxin
    • Bernardi, K.M.; Forster, M.L.; Lencer, W.I.; Tsai, B. Derlin-1 facilitates the retro-translocation of cholera toxin. Mol. Biol. Cell 2008, 19, 877-884.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 877-884
    • Bernardi, K.M.1    Forster, M.L.2    Lencer, W.I.3    Tsai, B.4
  • 77
    • 26444621357 scopus 로고    scopus 로고
    • Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • Ye, Y.; Shibata, Y.; Kikkert, M.; van Voorden, S.; Wiertz, E.; Rapoport, T.A. Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. USA 2005, 102, 14132-14138.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14132-14138
    • Ye, Y.1    Shibata, Y.2    Kikkert, M.3    Van Voorden, S.4    Wiertz, E.5    Rapoport, T.A.6
  • 78
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda, Y.; Okada, T.; Yoshida, H.; Kaufman, R.J.; Nagata, K.; Mori, K. Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J. Cell Biol. 2006, 172, 383-393.
    • (2006) J. Cell Biol. , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 79
    • 26244466567 scopus 로고    scopus 로고
    • The retrotranslocation protein Derlin-1 binds peptide: N-glycanase to the endoplasmic reticulum
    • Katiyar, S.; Joshi, S.; Lennarz, W.J. The retrotranslocation protein Derlin-1 binds peptide: N-glycanase to the endoplasmic reticulum. Mol. Biol. Cell 2005, 16, 4584-4594.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4584-4594
    • Katiyar, S.1    Joshi, S.2    Lennarz, W.J.3
  • 80
    • 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
  • 81
    • 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
  • 82
    • 4444232905 scopus 로고    scopus 로고
    • The unfolded protein response-A stress signaling pathway of the endoplasmic reticulum
    • Shen, X.; Zhang, K.; Kaufman, R.J. The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum. J. Chem. Neuroanat. 2004, 28, 79-92.
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 79-92
    • Shen, X.1    Zhang, K.2    Kaufman, R.J.3
  • 83
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers, K.J.; Patil, C.K.; Wodicka, L.; Lockhart, D.J.; Weissman, J.S.; Walter, P. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 2000, 101, 249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 84
    • 43249109174 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses
    • Schroder, M. Endoplasmic reticulum stress responses. Cell Mol. Life Sci. 2008, 65, 862-894.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 862-894
    • Schroder, M.1
  • 85
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells
    • Oyadomari, S.; Araki, E.; Mori, M. Endoplasmic reticulum stress-mediated apoptosis in pancreatic β-cells. Apoptosis 2002, 7, 335-345.
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 86
    • 0037166303 scopus 로고    scopus 로고
    • The protein kinase/endoribonuclease IRE1α that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain
    • Liu, C.Y.; Wong, H.N.; Schauerte, J.A.; Kaufman, R.J. The protein kinase/endoribonuclease IRE1α that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain. J. Biol. Chem. 2002, 277, 18346-18356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18346-18356
    • Liu, C.Y.1    Wong, H.N.2    Schauerte, J.A.3    Kaufman, R.J.4
  • 87
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang, K.; Kaufman, R.J. Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb. Exp. Pharmacol. 2006, 69-91.
    • (2006) Handb. Exp. Pharmacol , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 88
    • 15944369290 scopus 로고    scopus 로고
    • ER stress signaling by regulated splicing: IRE1/HAC1/XBP1
    • Back, S.H.; Schroder, M.; Lee, K.; Zhang, K.; Kaufman, R.J. ER stress signaling by regulated splicing: IRE1/HAC1/XBP1. Methods 2005, 35, 395-416.
    • (2005) Methods , vol.35 , pp. 395-416
    • Back, S.H.1    Schroder, M.2    Lee, K.3    Zhang, K.4    Kaufman, R.J.5
  • 89
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmicreticulum-resident kinase
    • Harding, H.P.; Zhang, Y.; Ron, D. Protein translation and folding are coupled by an endoplasmicreticulum-resident kinase. Nature 1999, 397, 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 90
  • 92
    • 33746500168 scopus 로고    scopus 로고
    • GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development
    • Luo, S.; Mao, C.; Lee, B.; Lee, A.S. GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development. Mol. Cell. Biol. 2006, 26, 5688-5697.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5688-5697
    • Luo, S.1    Mao, C.2    Lee, B.3    Lee, A.S.4
  • 93
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion
    • Wanderling, S.; Simen, B.B.; Ostrovsky, O.; Ahmed, N.T.; Vogen, S.M.; Gidalevitz, T.; Argon, Y. GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion. Mol. Biol. Cell 2007, 18, 3764-3775.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3764-3775
    • Wanderling, S.1    Simen, B.B.2    Ostrovsky, O.3    Ahmed, N.T.4    Vogen, S.M.5    Gidalevitz, T.6    Argon, Y.7
  • 94
    • 77949879489 scopus 로고    scopus 로고
    • ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum
    • Coe, H.; Jung, J.; Groenendyk, J.; Prins, D.; Michalak, M. ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J. Biol. Chem. 2010, 285, 6725-6738.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6725-6738
    • Coe, H.1    Jung, J.2    Groenendyk, J.3    Prins, D.4    Michalak, M.5
  • 96
    • 34547933706 scopus 로고    scopus 로고
    • Effects of the isoform-specific characteristics of ATF6α and ATF6β on endoplasmic reticulum stress response gene expression and cell viability
    • Thuerauf, D.J.; Marcinko, M.; Belmont, P.J.; Glembotski, C.C. Effects of the isoform-specific characteristics of ATF6α and ATF6β on endoplasmic reticulum stress response gene expression and cell viability. J. Biol. Chem. 2007, 282, 22865-22878.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22865-22878
    • Thuerauf, D.J.1    Marcinko, M.2    Belmont, P.J.3    Glembotski, C.C.4
  • 98
    • 4043076224 scopus 로고    scopus 로고
    • Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: Possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis
    • Okada, K.; Minamino, T.; Tsukamoto, Y.; Liao, Y.; Tsukamoto, O.; Takashima, S.; Hirata, A.; Fujita, M.; Nagamachi, Y.; Nakatani, T.; et al. Prolonged endoplasmic reticulum stress in hypertrophic and failing heart after aortic constriction: Possible contribution of endoplasmic reticulum stress to cardiac myocyte apoptosis. Circulation 2004, 110, 705-712.
    • (2004) Circulation , vol.110 , pp. 705-712
    • Okada, K.1    Minamino, T.2    Tsukamoto, Y.3    Liao, Y.4    Tsukamoto, O.5    Takashima, S.6    Hirata, A.7    Fujita, M.8    Nagamachi, Y.9    Nakatani, T.10
  • 99
    • 33745019669 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6
    • Martindale, J.J.; Fernandez, R.; Thuerauf, D.; Whittaker, R.; Gude, N.; Sussman, M.A.; Glembotski, C.C. Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6. Circ. Res. 2006, 98, 1186-1193.
    • (2006) Circ. Res. , vol.98 , pp. 1186-1193
    • Martindale, J.J.1    Fernandez, R.2    Thuerauf, D.3    Whittaker, R.4    Gude, N.5    Sussman, M.A.6    Glembotski, C.C.7
  • 100
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinson's disease
    • Mercado, G.; Valdes, P.; Hetz, C. An ERcentric view of Parkinson's disease. Trends Mol. Med. 2013, 19, 165-175.
    • (2013) Trends Mol. Med. , vol.19 , pp. 165-175
    • Mercado, G.1    Valdes, P.2    Hetz, C.3
  • 101
    • 84926343690 scopus 로고    scopus 로고
    • ER proteostasis disturbances in Parkinson's disease: Novel insights
    • Mercado, G.; Castillo, V.; Vidal, R.; Hetz, C. ER proteostasis disturbances in Parkinson's disease: Novel insights. Front. Aging Neurosci. 2015, 7, 39, doi:10.3389/fnagi.2015.00039.
    • (2015) Front. Aging Neurosci. , vol.7 , pp. 39
    • Mercado, G.1    Castillo, V.2    Vidal, R.3    Hetz, C.4
  • 102
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • Torres, M.; Castillo, K.; Armisen, R.; Stutzin, A.; Soto, C.; Hetz, C. Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS ONE 2010, 5, e15658.
    • (2010) PLoS ONE , vol.5 , pp. e15658
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 109
    • 84867006695 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress and the unfolded protein response in fibrosis
    • Lenna, S.; Trojanowska, M. The role of endoplasmic reticulum stress and the unfolded protein response in fibrosis. Curr. Opin. Rheumatol. 2012, 24, 663-668.
    • (2012) Curr. Opin. Rheumatol. , vol.24 , pp. 663-668
    • Lenna, S.1    Trojanowska, M.2
  • 110
    • 79960085864 scopus 로고    scopus 로고
    • Abnormal calcium homeostasis and protein folding stress at the ER: A common factor in familial and infectious prion disorders
    • Torres, M.; Encina, G.; Soto, C.; Hetz, C. Abnormal calcium homeostasis and protein folding stress at the ER: A common factor in familial and infectious prion disorders. Commun. Integr. Biol. 2011, 4, 258-261.
    • (2011) Commun. Integr. Biol. , vol.4 , pp. 258-261
    • Torres, M.1    Encina, G.2    Soto, C.3    Hetz, C.4
  • 111
    • 43549105167 scopus 로고    scopus 로고
    • The unfolded protein response: A pathway that links insulin demand with β-cell failure and diabetes
    • Scheuner, D.; Kaufman, R.J. The unfolded protein response: A pathway that links insulin demand with β-cell failure and diabetes. Endocr. Rev. 2008, 29, 317-333.
    • (2008) Endocr. Rev. , vol.29 , pp. 317-333
    • Scheuner, D.1    Kaufman, R.J.2
  • 112
    • 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


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