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Volumn 147, Issue 1, 2010, Pages 27-33

Stress-sensing mechanisms in the unfolded protein response: Similarities and differences between yeast and mammals

Author keywords

BiP; Clustering; ER stress sensor; IRE1; Unfolded protein response

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 6; GLUCOSE REGULATED PROTEIN 78; PROTEIN IRE1; PROTEIN KINASE; PROTEIN PERK; UNCLASSIFIED DRUG;

EID: 75649118565     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp196     Document Type: Short Survey
Times cited : (91)

References (52)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J. and Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and Helenius, A. (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
  • 3
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 4
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M. and Kaufman, R.J. (2005) The mammalian unfolded protein response. Annu. Rev. Biochem. 74, 739-789
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 5
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome
    • Hetz, C. and Glimcher, L.H. (2009) Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol. Cell 35, 551-561
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 6
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J.S., Shamu, C.E., and Walter, P. (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 7
    • 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., Ma, W., Gething, M.J., and Sambrook, J. (1993) A transmembrane protein with a cdc2+/ CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743-756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 8
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding, H.P., Zhang, Y., and Ron, D. (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 9
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi, Y., Vattem, K.M., Sood, R., An, J., Liang, J., Stramm, L., and Wek, R.C. (1998) Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol. Cell. Biol. 18, 7499-7509
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3    An, J.4    Liang, J.5    Stramm, L.6    Wek, R.C.7
  • 10
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K., Yoshida, H., Yanagi, H., Yura, T., and Mori, K. (1999) Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 10, 3787-3799
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 11
    • 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., Welihinda, A.A., and Kaufman, R.J. (1998) 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, 1812-1824
    • (1998) Genes Dev. , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 12
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang, X.Z., Harding, H.P., Zhang, Y., Jolicoeur, E.M., Kuroda, M., and Ron, D. (1998) Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17, 5708-5717
    • (1998) EMBO J. , vol.17 , pp. 5708-5717
    • Wang, X.Z.1    Harding, H.P.2    Zhang, Y.3    Jolicoeur, E.M.4    Kuroda, M.5    Ron, D.6
  • 14
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu, C.E. and Walter, P. (1996) Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028-3039
    • (1996) EMBO J. , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 15
    • 0029892851 scopus 로고    scopus 로고
    • The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation
    • Welihinda, A.A. and Kaufman, R.J. (1996) The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271, 18181-18187
    • (1996) J. Biol. Chem. , vol.271 , pp. 18181-18187
    • Welihinda, A.A.1    Kaufman, R.J.2
  • 16
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J.S. and Walter, P. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 17
    • 0030228708 scopus 로고    scopus 로고
    • Signalling from endoplasmic reticulum to nucleus: Transcription factor with a basic-leucine zipper motif is required for the unfolded proteinresponse pathway
    • Mori, K., Kawahara, T., Yoshida, H., Yanagi, H., and Yura, T. (1996) Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded proteinresponse pathway. Genes Cells 1, 803-817
    • (1996) Genes Cells , vol.1 , pp. 803-817
    • Mori, K.1    Kawahara, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5
  • 18
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., and Mori, K. (2001) XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881-891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 19
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M., Zeng, H., Urano, F., Till, J.H., Hubbard, S.R., Harding, H.P., Clark, S.G., and Ron, D. (2002) IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 415, 92-96
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 20
    • 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., and Walter, P. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 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
  • 21
    • 33645866473 scopus 로고    scopus 로고
    • Yeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins
    • Kimata, Y., Ishiwata-Kimata, Y., Yamada, S., and Kohno, K. (2006) Yeast unfolded protein response pathway regulates expression of genes for anti-oxidative stress and for cell surface proteins. Genes Cells 11, 59-69
    • (2006) Genes Cells , vol.11 , pp. 59-69
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Yamada, S.3    Kohno, K.4
  • 22
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A.H., Iwakoshi, N.N., and Glimcher, L.H. (2003) XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 23
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye, J., Rawson, R.B., Komuro, R., Chen, X., Dave, U.P., Prywes, R., Brown, M.S., and Goldstein, J.L. (2000) ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol. Cell 6, 1355-1364
    • (2000) Mol. Cell , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3    Chen, X.4    Dave, U.P.5    Prywes, R.6    Brown, M.S.7    Goldstein, J.L.8
  • 24
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada, T., Yoshida, H., Akazawa, R., Negishi, M., and Mori, K. (2002) Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366, 585-594
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 26
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • Adachi, Y., Yamamoto, K., Okada, T., Yoshida, H., Harada, A., and Mori, K. (2008) ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct. Funct. 33, 75-89
    • (2008) Cell Struct. Funct. , vol.33 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 27
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas, I.G. and Wabl, M. (1983) Immunoglobulin heavy chain binding protein. Nature 306, 387-389
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 28
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.J., and Sambrook, J. (1989) S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 29
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Zhang, Y., Hendershot, L.M., Harding, H.P., and Ron, D. (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
  • 30
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura, K., Kimata, Y., Higashio, H., Tsuru, A., and Kohno, K. (2000) Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279, 445-450
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 31
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., Chen, X., Hendershot, L., and Prywes, R. (2002) ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell. 3, 99-111
    • (2002) Dev. Cell. , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 32
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata, Y., Oikawa, D., Shimizu, Y., Ishiwata- Kimata, Y., and Kohno, K. (2004) A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell Biol. 167, 445-456
    • (2004) J. Cell Biol. , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata- Kimata, Y.4    Kohno, K.5
  • 33
    • 26844439863 scopus 로고    scopus 로고
    • An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1
    • Oikawa, D., Kimata, Y., Takeuchi, M., and Kohno, K. (2005) An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1. Biochem. J. 391, 135-142
    • (2005) Biochem. J. , vol.391 , pp. 135-142
    • Oikawa, D.1    Kimata, Y.2    Takeuchi, M.3    Kohno, K.4
  • 34
    • 34249707984 scopus 로고    scopus 로고
    • Selfassociation and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1
    • Oikawa, D., Kimata, Y., and Kohno, K. (2007) Selfassociation and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1. J. Cell. Sci. 120, 1681-1688
    • (2007) J. Cell. Sci. , vol.120 , pp. 1681-1688
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3
  • 36
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., Takeuchi, M., and Kohno, K. (2007) Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell Biol. 179, 75-86
    • (2007) J. Cell Biol. , vol.179 , pp. 75-86
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Ito, T.3    Hirata, A.4    Suzuki, T.5    Oikawa, D.6    Takeuchi, M.7    Kohno, K.8
  • 37
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou, J., Liu, C.Y., Back, S.H., Clark, R.L., Peisach, D., Xu, Z., and Kaufman, R.J. (2006) The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc. Natl Acad. Sci. USA 103, 14343-14348
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7
  • 38
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu, C.Y., Schroder, M., and Kaufman, R.J. (2000) Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 275, 24881-24885
    • (2000) J. Biol. Chem. , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 39
    • 0037166303 scopus 로고    scopus 로고
    • The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligandindependent dimerization domain
    • Liu, C.Y., Wong, H.N., Schauerte, J.A., and Kaufman, R.J. (2002) The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligandindependent dimerization domain. J. Biol. Chem. 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
  • 40
    • 67651045789 scopus 로고    scopus 로고
    • Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins
    • Oikawa, D., Kimata, Y., Kohno, K., and Iwawaki, T. (2009) Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins. Exp. Cell Res. 315, 2496-2504
    • (2009) Exp. Cell Res. , vol.315 , pp. 2496-2504
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3    Iwawaki, T.4
  • 43
    • 64749103329 scopus 로고    scopus 로고
    • Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA
    • Yanagitani, K., Imagawa, Y., Iwawaki, T., Hosoda, A., Saito, M., Kimata, Y., and Kohno, K. (2009) Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA. Mol. Cell 34, 191-200
    • (2009) Mol. Cell , vol.34 , pp. 191-200
    • Yanagitani, K.1    Imagawa, Y.2    Iwawaki, T.3    Hosoda, A.4    Saito, M.5    Kimata, Y.6    Kohno, K.7
  • 44
    • 0035812716 scopus 로고    scopus 로고
    • Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response
    • Ruegsegger, U., Leber, J.H., and Walter, P. (2001) Block of HAC1 mRNA translation by long-range base pairing is released by cytoplasmic splicing upon induction of the unfolded protein response. Cell 107, 103-114
    • (2001) Cell , vol.107 , pp. 103-114
    • Ruegsegger, U.1    Leber, J.H.2    Walter, P.3
  • 45
    • 32644432826 scopus 로고    scopus 로고
    • PXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response
    • Yoshida, H., Oku, M., Suzuki, M., and Mori, K. (2006) pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response. J. Cell Biol. 172, 565-575
    • (2006) J. Cell Biol. , vol.172 , pp. 565-575
    • Yoshida, H.1    Oku, M.2    Suzuki, M.3    Mori, K.4
  • 46
    • 63649157914 scopus 로고    scopus 로고
    • PXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation
    • Yoshida, H., Uemura, A., and Mori, K. (2009) pXBP1(U), a negative regulator of the unfolded protein response activator pXBP1(S), targets ATF6 but not ATF4 in proteasome-mediated degradation. Cell Struct. Funct. 34, 1-10
    • (2009) Cell Struct. Funct. , vol.34 , pp. 1-10
    • Yoshida, H.1    Uemura, A.2    Mori, K.3
  • 47
    • 64749096382 scopus 로고    scopus 로고
    • Targeting of mRNAs to their sites of unconventional splicing in the unfolded protein response
    • Ron, D. (2009) Targeting of mRNAs to their sites of unconventional splicing in the unfolded protein response. Mol. Cell 34, 133-134
    • (2009) Mol. Cell , vol.34 , pp. 133-134
    • Ron, D.1
  • 48
    • 0037166237 scopus 로고    scopus 로고
    • Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress
    • Ma, K., Vattem, K.M., and Wek, R.C. (2002) Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress. J. Biol. Chem. 277, 18728-18735
    • (2002) J. Biol. Chem. , vol.277 , pp. 18728-18735
    • Ma, K.1    Vattem, K.M.2    Wek, R.C.3
  • 49
    • 33846187752 scopus 로고    scopus 로고
    • Reduction of disulfide bridges in the lumenal domain of ATF6 in response to glucose starvation
    • Nadanaka, S., Yoshida, H., and Mori, K. (2006) Reduction of disulfide bridges in the lumenal domain of ATF6 in response to glucose starvation. Cell Struct. Funct. 31, 127-134
    • (2006) Cell Struct. Funct. , vol.31 , pp. 127-134
    • Nadanaka, S.1    Yoshida, H.2    Mori, K.3
  • 50
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • Nadanaka, S., Okada, T., Yoshida, H., and Mori, K. (2007) Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Mol. Cell. Biol. 27, 1027-1043
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 51
    • 70449577164 scopus 로고    scopus 로고
    • In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles
    • Schindler, A.J. and Schekman, R. (2009) In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles. Proc. Natl Acad. Sci. USA 106, 17775-17780
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 17775-17780
    • Schindler, A.J.1    Schekman, R.2
  • 52
    • 35348951126 scopus 로고    scopus 로고
    • How transmembrane proteins sense endoplasmic reticulum stress
    • Kohno, K. (2007) How transmembrane proteins sense endoplasmic reticulum stress. Antioxid. Redox Signal. 9, 2295-2303
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2295-2303
    • Kohno, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.