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Volumn 19, Issue 12, 2012, Pages 1939-1949

Activation of OASIS family, ER stress transducers, is dependent on its stabilization

Author keywords

BBF2H7; degradation; ER stress response; HRD1; OASIS

Indexed keywords

BBF2 HUMAN HOMOLOG ON CHROMOSOME 7; COLLAGEN; MEMBRANE PROTEIN; OLD ASTROCYTE SPECIFICALLY INDUCED SUBSTANCE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; X BOX BINDING PROTEIN 1;

EID: 84869090772     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2012.77     Document Type: Article
Times cited : (47)

References (38)
  • 1
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8: 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 2
    • 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 JH, Hubbard SR, Harding HP et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002; 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
  • 3
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum- resident kinase
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397: 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 4
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H, Okada T, Haze K, Yanagi H, Yura T, Negishi M et al. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol Cell Biol 2000; 20: 6755-6767.
    • (2000) Mol Cell Biol , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6
  • 5
    • 0036069980 scopus 로고    scopus 로고
    • Stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes RER. stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 2002; 3: 99-111.
    • (2002) Dev Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.E.R.4
  • 6
    • 79954490167 scopus 로고    scopus 로고
    • Physiological unfolded protein response regulated by CREB/ATF family members, transmembrane bZIP transcription factors
    • Kondo S, Saito A, Asada R, Kanemoto S, Imaizumi K. Physiological unfolded protein response regulated by CREB/ATF family members, transmembrane bZIP transcription factors. IUBMB Life 2011; 63: 233-239.
    • (2011) IUBMB Life , vol.63 , pp. 233-239
    • Kondo, S.1    Saito, A.2    Asada, R.3    Kanemoto, S.4    Imaizumi, K.5
  • 7
    • 79955424672 scopus 로고    scopus 로고
    • The signaling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellullar physiology
    • Asada R, Kanemoto S, Kondo S, Saito A, Imaizumi K. The signaling from endoplasmic reticulum-resident bZIP transcription factors involved in diverse cellullar physiology. J Biochem 2011; 149: 507-518.
    • (2011) J Biochem , vol.149 , pp. 507-518
    • Asada, R.1    Kanemoto, S.2    Kondo, S.3    Saito, A.4    Imaizumi, K.5
  • 10
    • 33847188475 scopus 로고    scopus 로고
    • BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer
    • Kondo S, Saito A, Hino S-I, Murakami T, Ogata M, Kanemoto S et al. BBF2H7, a novel transmembrane bZIP transcription factor, is a new type of endoplasmic reticulum stress transducer. Mol Cell Biol 2007; 27: 1716-1729.
    • (2007) Mol Cell Biol , vol.27 , pp. 1716-1729
    • Kondo, S.1    Saito, A.2    Hino, S.-I.3    Murakami, T.4    Ogata, M.5    Kanemoto, S.6
  • 11
    • 32044453080 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response
    • Zhang K, Shen X, Wu J, Sakaki K, Saunders T, Rutkowski DT et al. Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. Cell 2006; 124: 587-599.
    • (2006) Cell , vol.124 , pp. 587-599
    • Zhang, K.1    Shen, X.2    Wu, J.3    Sakaki, K.4    Saunders, T.5    Rutkowski, D.T.6
  • 12
    • 20944445990 scopus 로고    scopus 로고
    • Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway
    • Nagamori I, Yabuta N, Fujii T, Tanaka H, Yomogida K, Nishimune Y et al. Tisp40, a spermatid specific bZip transcription factor, functions by binding to the unfolded protein response element via the Rip pathway. Genes Cells 2005; 10: 575-594.
    • (2005) Genes Cells , vol.10 , pp. 575-594
    • Nagamori, I.1    Yabuta, N.2    Fujii, T.3    Tanaka, H.4    Yomogida, K.5    Nishimune, Y.6
  • 13
    • 30044441047 scopus 로고    scopus 로고
    • CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P
    • Stirling J, O'Hare P. CREB4, a transmembrane bZip transcription factor and potential new substrate for regulation and cleavage by S1P. Mol Biol Cell 2006; 17: 413-426.
    • (2006) Mol Biol Cell , vol.17 , pp. 413-426
    • Stirling, J.1    O'hare, P.2
  • 14
    • 70349652275 scopus 로고    scopus 로고
    • Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation
    • Murakami T, Saito A, Hino S-I, Kondo S, Kanemoto S, Chihara K et al. Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation. Nat Cell Biol 2009; 11: 1205-1211.
    • (2009) Nat Cell Biol , vol.11 , pp. 1205-1211
    • Murakami, T.1    Saito, A.2    Hino, S.-I.3    Kondo, S.4    Kanemoto, S.5    Chihara, K.6
  • 15
    • 70349652454 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum stress response by a BBF2H7-mediated Sec23a pathway is essential for chondrogenesis
    • Saito A, Hino S-I, Murakami T, Kanemoto S, Kondo S, Saitoh M et al. Regulation of endoplasmic reticulum stress response by a BBF2H7-mediated Sec23a pathway is essential for chondrogenesis. Nat Cell Biol 2009; 11: 1197-1204.
    • (2009) Nat Cell Biol , vol.11 , pp. 1197-1204
    • Saito, A.1    Hino, S.-I.2    Murakami, T.3    Kanemoto, S.4    Kondo, S.5    Saitoh, M.6
  • 16
    • 18444366176 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel human cAMP response element-binding (CREB) gene (CREB4)
    • Cao G, Ni X, Jiang M, Ma Y, Cheng H, Guo L et al. Molecular cloning and characterization of a novel human cAMP response element-binding (CREB) gene (CREB4). J Hum Genet 2002; 47: 373-376.
    • (2002) J Hum Genet , vol.47 , pp. 373-376
    • Cao, G.1    Ni, X.2    Jiang, M.3    Ma, Y.4    Cheng, H.5    Guo, L.6
  • 17
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB, Goldstein JL. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 2000; 100: 391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 18
    • 35848940511 scopus 로고    scopus 로고
    • Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response
    • Bailey D, O'Hare P. Transmembrane bZIP transcription factors in ER stress signaling and the unfolded protein response. Antioxid Redox Signal 2007; 9: 2305-2321.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2305-2321
    • Bailey, D.1    O'hare, P.2
  • 19
    • 33645107263 scopus 로고    scopus 로고
    • Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress
    • Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A et al. Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem 2006; 96: 1090-1100.
    • (2006) J Neurochem , vol.96 , pp. 1090-1100
    • Murakami, T.1    Kondo, S.2    Ogata, M.3    Kanemoto, S.4    Saito, A.5    Wanaka, A.6
  • 20
    • 18844429239 scopus 로고    scopus 로고
    • Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells
    • Chen C, Sun X, Ran Q, Wilkinson KD, Murphy TJ, Simons JW et al. Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells. Oncogene 2005; 24: 3319-3327.
    • (2005) Oncogene , vol.24 , pp. 3319-3327
    • Chen, C.1    Sun, X.2    Ran, Q.3    Wilkinson, K.D.4    Murphy, T.J.5    Simons, J.W.6
  • 21
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart CM. Back to the future with ubiquitin. Cell 116: 181-190.
    • Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 22
    • 77949751415 scopus 로고    scopus 로고
    • Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells
    • Fonseca SG, Ishigaki S, Oslowski CM, Lu S, Lipson KL, Ghosh R et al. Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells. J Clin Invest 2010; 120: 744-755.
    • (2010) J Clin Invest , vol.120 , pp. 744-755
    • Fonseca, S.G.1    Ishigaki, S.2    Oslowski, C.M.3    Lu, S.4    Lipson, K.L.5    Ghosh, R.6
  • 23
    • 79955536632 scopus 로고    scopus 로고
    • The IRE1a-XBP1 pathway is essential for osteoblast differentiation through promoting transcription of Osterix
    • Tohmonda T, Miyauchi Y, Ghosh R, Yoda M, Uchikawa S, Takito J et al. The IRE1a-XBP1 pathway is essential for osteoblast differentiation through promoting transcription of Osterix. EMBO Rep 2011; 12: 451-457.
    • (2011) EMBO Rep , vol.12 , pp. 451-457
    • Tohmonda, T.1    Miyauchi, Y.2    Ghosh, R.3    Yoda, M.4    Uchikawa, S.5    Takito, J.6
  • 24
    • 10744222535 scopus 로고    scopus 로고
    • Synoviolin/ Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy
    • Amano T, Yamasaki S, Yagishita N, Tsuchimochi K, Shin H, Kawahara K et al. Synoviolin/ Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathy. Genes Dev 2003; 17: 2436-2449.
    • (2003) Genes Dev , vol.17 , pp. 2436-2449
    • Amano, T.1    Yamasaki, S.2    Yagishita, N.3    Tsuchimochi, K.4    Shin, H.5    Kawahara, K.6
  • 25
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1- antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR. OS-9 and GRP94 deliver mutant alpha1- 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
  • 26
    • 33845536214 scopus 로고    scopus 로고
    • A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin
    • Omura T, Kaneko M, Okuma Y, Orba Y, Nagashima K, Takahashi R et al. A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. J Neurochem 2006; 99: 1456-1469.
    • (2006) J Neurochem , vol.99 , pp. 1456-1469
    • Omura, T.1    Kaneko, M.2    Okuma, Y.3    Orba, Y.4    Nagashima, K.5    Takahashi, R.6
  • 27
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation
    • Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y, Nomura Y. Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J Neurosci 2010; 30: 3924-3932.
    • (2010) J Neurosci , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 28
    • 78751703950 scopus 로고    scopus 로고
    • Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution
    • Taguchi K, Motohashi H, Yamamoto M. Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution. Genes Cells 2011; 16: 123-140.
    • (2011) Genes Cells , vol.16 , pp. 123-140
    • Taguchi, K.1    Motohashi, H.2    Yamamoto, M.3
  • 29
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • DeBose-Boyd RA, Brown MS, Li WP, Nohturfft A, Goldstein JL, Espenshade PJ. Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi. Cell 1999; 99: 703-712.
    • (1999) Cell , vol.99 , pp. 703-712
    • Debose-Boyd, R.A.1    Brown, M.S.2    Li, W.P.3    Nohturfft, A.4    Goldstein, J.L.5    Espenshade, P.J.6
  • 30
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002; 110: 489-500.
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3    Yabe, D.4    Gong, Y.5    Aebersold, R.6
  • 31
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • Brown AJ, Sun L, Feramisco JD, Brown MS, Goldstein JL. Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol Cell 2002; 10: 237-245.
    • (2002) Mol Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 32
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: Mechanism for a sterol-sensing domain
    • Radhakrishnan A, Sun LP, Kwon HJ, Brown MS, Goldstein JL. Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Mol Cell 2004; 15: 259-268.
    • (2004) Mol Cell , vol.15 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 33
    • 41149125522 scopus 로고    scopus 로고
    • Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation
    • Li JG, Haines DS, Liu-Chen LY. Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation. Mol Pharmacol 2008; 73: 1319-1330.
    • (2008) Mol Pharmacol , vol.73 , pp. 1319-1330
    • Li, J.G.1    Haines, D.S.2    Liu-Chen, L.Y.3
  • 34
    • 41549116799 scopus 로고    scopus 로고
    • Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains
    • Omura T, Kaneko M, Onoguchi M, Koizumi S, Itami M, Ueyama M et al. Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains. J Pharmacol Sci 2008; 106: 512-519.
    • (2008) J Pharmacol Sci , vol.106 , pp. 512-519
    • Omura, T.1    Kaneko, M.2    Onoguchi, M.3    Koizumi, S.4    Itami, M.5    Ueyama, M.6
  • 35
    • 33846219143 scopus 로고    scopus 로고
    • Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'
    • Yamasaki S, Yagishita N, Sasaki T, Nakazawa M, Kato Y, Yamadera T et al. Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'. EMBO J 2007; 26: 113-122.
    • (2007) EMBO J , vol.26 , pp. 113-122
    • Yamasaki, S.1    Yagishita, N.2    Sasaki, T.3    Nakazawa, M.4    Kato, Y.5    Yamadera, T.6
  • 37
    • 0018573272 scopus 로고
    • Early events in the biosynthesis of the lysosomal enzyme Cathepsin D
    • Erickson AH, Blobel G. Early events in the biosynthesis of the lysosomal enzyme Cathepsin D. J Biol Chem 1979; 254: 11771-11774.
    • (1979) J Biol Chem , vol.254 , pp. 11771-11774
    • Erickson, A.H.1    Blobel, G.2
  • 38
    • 0030854775 scopus 로고    scopus 로고
    • Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death
    • Imaizumi K, Tsuda M, Imai Y, Wanaka A, Takagi T, Tohyama M. Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death. J Biol Chem 1997; 272: 18842-18848.
    • (1997) J Biol Chem , vol.272 , pp. 18842-18848
    • Imaizumi, K.1    Tsuda, M.2    Imai, Y.3    Wanaka, A.4    Takagi, T.5    Tohyama, M.6


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