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Volumn 27, Issue 6, 2017, Pages 430-440

New Insights into the Physiological Role of Endoplasmic Reticulum-Associated Degradation

Author keywords

[No Author keywords available]

Indexed keywords

HRD1 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 85010583779     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2016.12.002     Document Type: Review
Times cited : (181)

References (85)
  • 2
    • 84860118506 scopus 로고    scopus 로고
    • The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology
    • Guerriero, C.J., Brodsky, J.L., The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology. Physiol. Rev. 92 (2012), 537–576.
    • (2012) Physiol. Rev. , vol.92 , pp. 537-576
    • Guerriero, C.J.1    Brodsky, J.L.2
  • 3
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz, C., The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13 (2012), 89–102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 4
    • 80052366845 scopus 로고    scopus 로고
    • Stressed out about obesity: IRE1alpha-XBP1 in metabolic disorders
    • Sha, H., et al. Stressed out about obesity: IRE1alpha-XBP1 in metabolic disorders. Trends Endocrinol. Metab. 22 (2011), 374–381.
    • (2011) Trends Endocrinol. Metab. , vol.22 , pp. 374-381
    • Sha, H.1
  • 5
    • 20044394518 scopus 로고    scopus 로고
    • Essential role of synoviolin in embryogenesis
    • Yagishita, N., et al. Essential role of synoviolin in embryogenesis. J. Biol. Chem. 280 (2005), 7909–7916.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7909-7916
    • Yagishita, N.1
  • 6
    • 77951564358 scopus 로고    scopus 로고
    • Deficiency of suppressor enhancer lin12 1 like (SEL1L) in mice leads to systemic endoplasmic reticulum stress and embryonic lethality
    • Francisco, A.B., et al. Deficiency of suppressor enhancer lin12 1 like (SEL1L) in mice leads to systemic endoplasmic reticulum stress and embryonic lethality. J. Biol. Chem. 285 (2010), 13694–13703.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13694-13703
    • Francisco, A.B.1
  • 7
    • 33846506651 scopus 로고    scopus 로고
    • Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality
    • Müller, J.M., et al. Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality. Biochem. Biophys. Res. Commun. 354 (2007), 459–465.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 459-465
    • Müller, J.M.1
  • 8
    • 84896270715 scopus 로고    scopus 로고
    • Quality control: ER-associated degradation: protein quality control and beyond
    • Ruggiano, A., et al. Quality control: ER-associated degradation: protein quality control and beyond. J. Cell. Biol. 204 (2014), 869–879.
    • (2014) J. Cell. Biol. , vol.204 , pp. 869-879
    • Ruggiano, A.1
  • 9
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: ubiquitin in charge
    • Christianson, J.C., Ye, Y., Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nat. Struct. Mol. Biol. 21 (2014), 325–335.
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 10
    • 84979077635 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation and lipid homeostasis
    • Stevenson, J., et al. Endoplasmic reticulum-associated degradation and lipid homeostasis. Annu. Rev. Nutr. 36 (2016), 511–542.
    • (2016) Annu. Rev. Nutr. , vol.36 , pp. 511-542
    • Stevenson, J.1
  • 11
    • 84913536702 scopus 로고    scopus 로고
    • The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism
    • Sha, H., et al. The ER-associated degradation adaptor protein Sel1L regulates LPL secretion and lipid metabolism. Cell Metab. 20 (2014), 458–470.
    • (2014) Cell Metab. , vol.20 , pp. 458-470
    • Sha, H.1
  • 12
    • 84893517295 scopus 로고    scopus 로고
    • Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival
    • Sun, S., et al. Sel1L is indispensable for mammalian endoplasmic reticulum-associated degradation, endoplasmic reticulum homeostasis, and survival. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), E582–E591.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E582-E591
    • Sun, S.1
  • 13
    • 84948712979 scopus 로고    scopus 로고
    • IRE1a is an endogenous substrate of endoplasmic-reticulum-associated degradation
    • Sun, S., et al. IRE1a is an endogenous substrate of endoplasmic-reticulum-associated degradation. Nat. Cell Biol. 17 (2015), 1546–1555.
    • (2015) Nat. Cell Biol. , vol.17 , pp. 1546-1555
    • Sun, S.1
  • 14
    • 84956634517 scopus 로고    scopus 로고
    • Epithelial Sel1L is required for the maintenance of intestinal homeostasis
    • Sun, S., et al. Epithelial Sel1L is required for the maintenance of intestinal homeostasis. Mol. Biol. Cell 27 (2016), 483–490.
    • (2016) Mol. Biol. Cell , vol.27 , pp. 483-490
    • Sun, S.1
  • 15
    • 84898874270 scopus 로고    scopus 로고
    • Hrd1 suppresses Nrf2-mediated cellular protection during liver cirrhosis
    • Wu, T., et al. Hrd1 suppresses Nrf2-mediated cellular protection during liver cirrhosis. Genes Dev. 28 (2014), 708–722.
    • (2014) Genes Dev. , vol.28 , pp. 708-722
    • Wu, T.1
  • 16
    • 84911924274 scopus 로고    scopus 로고
    • Hrd1-mediated BLIMP-1 ubiquitination promotes dendritic cell MHCII expression for CD4 T cell priming during inflammation
    • Yang, H., et al. Hrd1-mediated BLIMP-1 ubiquitination promotes dendritic cell MHCII expression for CD4 T cell priming during inflammation. J. Exp. Med. 211 (2014), 2467–2479.
    • (2014) J. Exp. Med. , vol.211 , pp. 2467-2479
    • Yang, H.1
  • 17
    • 84927698900 scopus 로고    scopus 로고
    • The E3 ligase synoviolin controls body weight and mitochondrial biogenesis through negative regulation of PGC-1beta
    • Fujita, H., et al. The E3 ligase synoviolin controls body weight and mitochondrial biogenesis through negative regulation of PGC-1beta. EMBO J. 34 (2015), 1042–1055.
    • (2015) EMBO J. , vol.34 , pp. 1042-1055
    • Fujita, H.1
  • 18
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., et al. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995), 121–127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1
  • 19
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C.L., Kopito, R.R., Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269 (1994), 25710–25718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 20
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs, G.L., et al. Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP. EMBO J. 13 (1994), 6076–6086.
    • (1994) EMBO J. , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1
  • 21
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R.Y., et al. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7 (1996), 2029–2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1
  • 22
    • 0034597161 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p
    • Gardner, R.G., et al. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J. Cell Biol. 151 (2000), 69–82.
    • (2000) J. Cell Biol. , vol.151 , pp. 69-82
    • Gardner, R.G.1
  • 23
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays, N.W., et al. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 3 (2001), 24–29.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1
  • 24
    • 0034971386 scopus 로고    scopus 로고
    • In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation
    • Gardner, R.G., et al. In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol. Cell Biol. 21 (2001), 4276–4291.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 4276-4291
    • Gardner, R.G.1
  • 25
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito, R.R., Biosynthesis and degradation of CFTR. Physiol. Rev. 79 (1999), S167–S173.
    • (1999) Physiol. Rev. , vol.79 , pp. S167-S173
    • Kopito, R.R.1
  • 26
    • 84870763849 scopus 로고    scopus 로고
    • The mammalian endoplasmic reticulum-associated degradation system
    • Olzmann, J.A., et al. The mammalian endoplasmic reticulum-associated degradation system. Cold Spring Harb. Perspect. Biol., 5, 2013, a013185.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a013185
    • Olzmann, J.A.1
  • 27
    • 84931565973 scopus 로고    scopus 로고
    • N-linked sugar-regulated protein folding and quality control in the ER
    • Tannous, A., et al. N-linked sugar-regulated protein folding and quality control in the ER. Semin. Cell Dev. Biol. 41 (2015), 79–89.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 79-89
    • Tannous, A.1
  • 28
    • 84870762133 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated degradation pathways of budding yeast
    • Thibault, G., Ng, D.T., The endoplasmic reticulum-associated degradation pathways of budding yeast. Cold Spring Harb. Perspect. Biol., 4, 2012, a013193.
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. a013193
    • Thibault, G.1    Ng, D.T.2
  • 29
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J.C., et al. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 10 (2008), 272–282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1
  • 30
    • 84970979593 scopus 로고    scopus 로고
    • Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway
    • Ninagawa, S., et al. Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway. J. Cell Biol. 211 (2015), 775–784.
    • (2015) J. Cell Biol. , vol.211 , pp. 775-784
    • Ninagawa, S.1
  • 31
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati, A., et al. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol. Cell 19 (2005), 741–751.
    • (2005) Mol. Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1
  • 32
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • Kim, W., et al. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol. Cell 19 (2005), 753–764.
    • (2005) Mol. Cell , vol.19 , pp. 753-764
    • Kim, W.1
  • 33
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari, M., et al. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299 (2003), 1397–1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1
  • 34
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda, Y., et al. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299 (2003), 1394–1397.
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1
  • 35
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R.K., et al. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388 (1997), 891–895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1
  • 36
    • 66449136067 scopus 로고    scopus 로고
    • EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex
    • Cormier, J.H., et al. EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Mol. Cell 34 (2009), 627–633.
    • (2009) Mol. Cell , vol.34 , pp. 627-633
    • Cormier, J.H.1
  • 37
    • 84255169603 scopus 로고    scopus 로고
    • Defining human ERAD networks through an integrative mapping strategy
    • Christianson, J.C., et al. Defining human ERAD networks through an integrative mapping strategy. Nat. Cell Biol. 14 (2012), 93–105.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 93-105
    • Christianson, J.C.1
  • 38
    • 33750359201 scopus 로고    scopus 로고
    • SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
    • Mueller, B., et al. SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J. Cell Biol. 175 (2006), 261–270.
    • (2006) J. Cell Biol. , vol.175 , pp. 261-270
    • Mueller, B.1
  • 39
    • 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. U. S. A. 102 (2005), 14296–14301.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 40
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • Mueller, B., et al. SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 12325–12330.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 12325-12330
    • Mueller, B.1
  • 41
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • Carvalho, P., et al. Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143 (2010), 579–591.
    • (2010) Cell , vol.143 , pp. 579-591
    • Carvalho, P.1
  • 42
    • 84978435047 scopus 로고    scopus 로고
    • Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD
    • Baldridge, R.D., Rapoport, T.A., Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD. Cell 166 (2016), 394–407.
    • (2016) Cell , vol.166 , pp. 394-407
    • Baldridge, R.D.1    Rapoport, T.A.2
  • 43
    • 84908072286 scopus 로고    scopus 로고
    • Key steps in ERAD of luminal ER proteins reconstituted with purified components
    • Stein, A., et al. Key steps in ERAD of luminal ER proteins reconstituted with purified components. Cell 158 (2014), 1375–1388.
    • (2014) Cell , vol.158 , pp. 1375-1388
    • Stein, A.1
  • 44
    • 84948978497 scopus 로고    scopus 로고
    • gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum
    • Zhang, T., et al. gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum. Mol. Biol. Cell 26 (2015), 4438–4450.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 4438-4450
    • Zhang, T.1
  • 45
    • 0027435169 scopus 로고
    • Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans
    • Sundaram, M., Greenwald, I., Suppressors of a lin-12 hypomorph define genes that interact with both lin-12 and glp-1 in Caenorhabditis elegans. Genetics 135 (1993), 765–783.
    • (1993) Genetics , vol.135 , pp. 765-783
    • Sundaram, M.1    Greenwald, I.2
  • 46
    • 84957812679 scopus 로고    scopus 로고
    • Crystal structure of SEL1L: insight into the roles of SLR motifs in ERAD pathway
    • Jeong, H., et al. Crystal structure of SEL1L: insight into the roles of SLR motifs in ERAD pathway. Sci. Rep., 6, 2016, 20261.
    • (2016) Sci. Rep. , vol.6 , pp. 20261
    • Jeong, H.1
  • 47
    • 79952433637 scopus 로고    scopus 로고
    • Processing and turnover of the Hedgehog protein in the endoplasmic reticulum
    • Chen, X., et al. Processing and turnover of the Hedgehog protein in the endoplasmic reticulum. J. Cell Biol. 192 (2011), 825–838.
    • (2011) J. Cell Biol. , vol.192 , pp. 825-838
    • Chen, X.1
  • 48
    • 84871197818 scopus 로고    scopus 로고
    • Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate
    • Tyler, R.E., et al. Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate. Mol. Biol. Cell 23 (2012), 4668–4678.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4668-4678
    • Tyler, R.E.1
  • 49
    • 84887058388 scopus 로고    scopus 로고
    • The unfolded protein response transducer ATF6 represents a novel transmembrane-type endoplasmic reticulum-associated degradation substrate requiring both mannose trimming and SEL1L protein
    • Horimoto, S., et al. The unfolded protein response transducer ATF6 represents a novel transmembrane-type endoplasmic reticulum-associated degradation substrate requiring both mannose trimming and SEL1L protein. J. Biol. Chem. 288 (2013), 31517–31527.
    • (2013) J. Biol. Chem. , vol.288 , pp. 31517-31527
    • Horimoto, S.1
  • 50
    • 79955758729 scopus 로고    scopus 로고
    • SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates
    • Iida, Y., et al. SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates. J. Biol. Chem. 286 (2011), 16929–16939.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16929-16939
    • Iida, Y.1
  • 51
    • 84875204546 scopus 로고    scopus 로고
    • The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation
    • Williams, J.M., et al. The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation. Mol. Biol. Cell 24 (2013), 785–795.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 785-795
    • Williams, J.M.1
  • 52
    • 84969749567 scopus 로고    scopus 로고
    • Direct and essential function for Hrd3 in ER-associated degradation
    • Vashistha, N., et al. Direct and essential function for Hrd3 in ER-associated degradation. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), 5934–5939.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. 5934-5939
    • Vashistha, N.1
  • 53
    • 84909962081 scopus 로고    scopus 로고
    • Quality control of inner nuclear membrane proteins by the Asi complex
    • Foresti, O., et al. Quality control of inner nuclear membrane proteins by the Asi complex. Science 346 (2014), 751–755.
    • (2014) Science , vol.346 , pp. 751-755
    • Foresti, O.1
  • 54
    • 84922218720 scopus 로고    scopus 로고
    • Protein quality control at the inner nuclear membrane
    • Khmelinskii, A., et al. Protein quality control at the inner nuclear membrane. Nature 516 (2014), 410–413.
    • (2014) Nature , vol.516 , pp. 410-413
    • Khmelinskii, A.1
  • 55
    • 84869464499 scopus 로고    scopus 로고
    • RING-finger type E3 ubiquitin ligase inhibitors as novel candidates for the treatment of rheumatoid arthritis
    • Yagishita, N., et al. RING-finger type E3 ubiquitin ligase inhibitors as novel candidates for the treatment of rheumatoid arthritis. Int. J. Mol. Med. 30 (2012), 1281–1286.
    • (2012) Int. J. Mol. Med. , vol.30 , pp. 1281-1286
    • Yagishita, N.1
  • 56
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori, K., et al. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74 (1993), 743–756.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1
  • 57
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa, J., Yamashita, S., IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol. Microbiol. 6 (1992), 1441–1446.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1441-1446
    • Nikawa, J.1    Yamashita, S.2
  • 58
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J.S., et al. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73 (1993), 1197–1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1
  • 59
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon, W., et al. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12 (1998), 1812–1824.
    • (1998) Genes Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1
  • 60
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang, X.Z., et al. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17 (1998), 5708–5717.
    • (1998) EMBO J. , vol.17 , pp. 5708-5717
    • Wang, X.Z.1
  • 61
    • 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., et al. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101 (2000), 249–258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1
  • 62
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida, H., et al. A time-dependent phase shift in the mammalian unfolded protein response. Dev. Cell 4 (2003), 265–271.
    • (2003) Dev. Cell , vol.4 , pp. 265-271
    • Yoshida, H.1
  • 63
    • 36049023152 scopus 로고    scopus 로고
    • A different pathway in the endoplasmic reticulum stress-induced expression of human HRD1 and SEL1 genes
    • Kaneko, M., et al. A different pathway in the endoplasmic reticulum stress-induced expression of human HRD1 and SEL1 genes. FEBS Lett. 581 (2007), 5355–5360.
    • (2007) FEBS Lett. , vol.581 , pp. 5355-5360
    • Kaneko, M.1
  • 64
    • 43049096083 scopus 로고    scopus 로고
    • Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis
    • Gao, B., et al. Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis. EMBO Rep. 9 (2008), 480–485.
    • (2008) EMBO Rep. , vol.9 , pp. 480-485
    • Gao, B.1
  • 65
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
    • Hayes, J.D., McMahon, M., NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer. Trends Biochem. Sci. 34 (2009), 176–188.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 66
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi, A., et al. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol. Cell Biol. 24 (2004), 7130–7139.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 7130-7139
    • Kobayashi, A.1
  • 67
    • 79952256187 scopus 로고    scopus 로고
    • SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner
    • Rada, P., et al. SCF/{beta}-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner. Mol. Cell Biol. 31 (2011), 1121–1133.
    • (2011) Mol. Cell Biol. , vol.31 , pp. 1121-1133
    • Rada, P.1
  • 68
    • 84978194206 scopus 로고    scopus 로고
    • Genome-wide association study in mice identifies loci affecting liver-related phenotypes including Sel1l influencing serum bile acids
    • Wu, W., et al. Genome-wide association study in mice identifies loci affecting liver-related phenotypes including Sel1l influencing serum bile acids. Hepatology 63 (2016), 1943–1956.
    • (2016) Hepatology , vol.63 , pp. 1943-1956
    • Wu, W.1
  • 69
    • 0029163399 scopus 로고
    • Genetics of responsiveness to high-fat and high-cholesterol diets in the mouse
    • Paigen, B., Genetics of responsiveness to high-fat and high-cholesterol diets in the mouse. Am. J. Clin. Nutr. 62 (1995), 458S–462S.
    • (1995) Am. J. Clin. Nutr. , vol.62 , pp. 458S-462S
    • Paigen, B.1
  • 70
    • 0003732734 scopus 로고    scopus 로고
    • Immunobiology: The Immune System in Health & Disease
    • 5th edn Garland Publishing Inc
    • Janeway, C.A. Jr, et al. Immunobiology: The Immune System in Health & Disease. 5th edn, 2001, Garland Publishing Inc, 7:1–7:35.
    • (2001) , pp. 71-7:35
    • Janeway, C.A.1
  • 71
    • 85002713183 scopus 로고    scopus 로고
    • The Sel1L-Hrd1 endoplasmic reticulum-associated degradation complex manages a key checkpoint in B cell development
    • Ji, Y., et al. The Sel1L-Hrd1 endoplasmic reticulum-associated degradation complex manages a key checkpoint in B cell development. Cell Rep. 16 (2016), 2630–2640.
    • (2016) Cell Rep. , vol.16 , pp. 2630-2640
    • Ji, Y.1
  • 72
    • 84873342483 scopus 로고    scopus 로고
    • Regulation of dendritic cell activation by microRNA let-7c and BLIMP1
    • Kim, S.J., et al. Regulation of dendritic cell activation by microRNA let-7c and BLIMP1. J. Clin. Invest. 123 (2013), 823–833.
    • (2013) J. Clin. Invest. , vol.123 , pp. 823-833
    • Kim, S.J.1
  • 73
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil, G., Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 140 (2010), 900–917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.1
  • 74
    • 77955342864 scopus 로고    scopus 로고
    • A Phos-tag-based method reveals the extent of physiological endoplasmic reticulum stress
    • Yang, L., et al. A Phos-tag-based method reveals the extent of physiological endoplasmic reticulum stress. PLoS One, 5, 2010, e11621.
    • (2010) PLoS One , vol.5 , pp. e11621
    • Yang, L.1
  • 75
    • 79251504265 scopus 로고    scopus 로고
    • Detecting and quantitating physiological endoplasmic reticulum stress
    • Qi, L., et al. Detecting and quantitating physiological endoplasmic reticulum stress. Methods Enzymol. 490 (2011), 137–146.
    • (2011) Methods Enzymol. , vol.490 , pp. 137-146
    • Qi, L.1
  • 76
    • 84938209174 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control in cancer: friend or foe
    • Kim, H., et al. Endoplasmic reticulum quality control in cancer: friend or foe. Semin. Cancer Biol. 33 (2015), 25–33.
    • (2015) Semin. Cancer Biol. , vol.33 , pp. 25-33
    • Kim, H.1
  • 77
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C elegans
    • David, D.C., et al. Widespread protein aggregation as an inherent part of aging in C elegans. PLoS Biol., 8, 2010, e1000450.
    • (2010) PLoS Biol. , vol.8 , pp. e1000450
    • David, D.C.1
  • 78
    • 17144365015 scopus 로고    scopus 로고
    • Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum
    • Liu, M., et al. Proinsulin disulfide maturation and misfolding in the endoplasmic reticulum. J. Biol. Chem. 280 (2005), 13209–13212.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13209-13212
    • Liu, M.1
  • 79
    • 67749096213 scopus 로고    scopus 로고
    • Proinsulin and the genetics of diabetes mellitus
    • Weiss, M.A., Proinsulin and the genetics of diabetes mellitus. J. Biol. Chem. 284 (2009), 19159–19163.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19159-19163
    • Weiss, M.A.1
  • 80
    • 84992268836 scopus 로고    scopus 로고
    • Mutations in the amino-terminal region of proopiomelanocortin (POMC) in patients with early-onset obesity impair POMC sorting to the regulated secretory pathway
    • Creemers, J.W., et al. Mutations in the amino-terminal region of proopiomelanocortin (POMC) in patients with early-onset obesity impair POMC sorting to the regulated secretory pathway. J. Clin. Endocrinol. Metab. 93 (2008), 4494–4499.
    • (2008) J. Clin. Endocrinol. Metab. , vol.93 , pp. 4494-4499
    • Creemers, J.W.1
  • 81
    • 70450230337 scopus 로고    scopus 로고
    • Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum
    • Birk, J., et al. Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum. J. Cell. Sci. 122 (2009), 3994–4002.
    • (2009) J. Cell. Sci. , vol.122 , pp. 3994-4002
    • Birk, J.1
  • 82
    • 2442475348 scopus 로고    scopus 로고
    • Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome
    • Friberg, M.A., et al. Degradation of wild-type vasopressin precursor and pathogenic mutants by the proteasome. J. Biol. Chem. 279 (2004), 19441–19447.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19441-19447
    • Friberg, M.A.1
  • 83
    • 84957801406 scopus 로고    scopus 로고
    • Thyroglobulin from molecular and cellular biology to clinical endocrinology
    • Di Jeso, B., Arvan, P., Thyroglobulin from molecular and cellular biology to clinical endocrinology. Endocr. Rev. 37 (2016), 2–36.
    • (2016) Endocr. Rev. , vol.37 , pp. 2-36
    • Di Jeso, B.1    Arvan, P.2
  • 84
    • 84962140678 scopus 로고    scopus 로고
    • Disulfide mispairing during proinsulin folding in the endoplasmic reticulum
    • Haataja, L., et al. Disulfide mispairing during proinsulin folding in the endoplasmic reticulum. Diabetes 65 (2016), 1050–1060.
    • (2016) Diabetes , vol.65 , pp. 1050-1060
    • Haataja, L.1
  • 85
    • 84943140507 scopus 로고    scopus 로고
    • PDI reductase acts on Akita mutant proinsulin to initiate retrotranslocation along the Hrd1/Sel1L-p97 axis
    • He, K., et al. PDI reductase acts on Akita mutant proinsulin to initiate retrotranslocation along the Hrd1/Sel1L-p97 axis. Mol. Biol. Cell 26 (2015), 3413–3423.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 3413-3423
    • He, K.1


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