메뉴 건너뛰기




Volumn 589, Issue 5, 2015, Pages 615-620

Induction of Herpud1 expression by ER stress is regulated by Nrf1

Author keywords

ER stress; Nuclear factor erythroid derived 2 related factor 1; Transcriptional regulation

Indexed keywords

HERPUD1 PROTEIN; MEMBRANE PROTEIN; TRANSCRIPTION FACTOR NRF1; UNCLASSIFIED DRUG; HERPUD1 PROTEIN, HUMAN; NUCLEAR RESPIRATORY FACTOR 1;

EID: 84922730667     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.01.026     Document Type: Article
Times cited : (35)

References (39)
  • 1
    • 0027243681 scopus 로고
    • Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein
    • N.C. Andrews, H. Erdjument-Bromage, M.B. Davidson, P. Tempst, and S.H. Orkin Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein Nature 362 1993 722 728
    • (1993) Nature , vol.362 , pp. 722-728
    • Andrews, N.C.1    Erdjument-Bromage, H.2    Davidson, M.B.3    Tempst, P.4    Orkin, S.H.5
  • 2
    • 0027360226 scopus 로고
    • Cloning of Nrf1, an NF-E2-related transcription factor, by genetic selection in yeast
    • J.Y. Chan, X.L. Han, and Y.W. Kan Cloning of Nrf1, an NF-E2-related transcription factor, by genetic selection in yeast Proc. Natl. Acad. Sci. U.S.A. 90 1993 11371 11375
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11371-11375
    • Chan, J.Y.1    Han, X.L.2    Kan, Y.W.3
  • 3
    • 0032536783 scopus 로고    scopus 로고
    • Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice
    • J.Y. Chan, M. Kwong, R. Lu, J. Chang, B. Wang, T.S. Yen, and Y.W. Kan Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice EMBO J. 17 1998 1779 1787
    • (1998) EMBO J. , vol.17 , pp. 1779-1787
    • Chan, J.Y.1    Kwong, M.2    Lu, R.3    Chang, J.4    Wang, B.5    Yen, T.S.6    Kan, Y.W.7
  • 6
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • C. Hetz 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
  • 8
    • 84894199319 scopus 로고    scopus 로고
    • Role of HERP and a HERP-related protein in HRD1-dependent protein degradation at the endoplasmic reticulum
    • C.H. Huang, Y.R. Chu, Y. Ye, and X. Chen Role of HERP and a HERP-related protein in HRD1-dependent protein degradation at the endoplasmic reticulum J. Biol. Chem. 289 2014 4444 4454
    • (2014) J. Biol. Chem. , vol.289 , pp. 4444-4454
    • Huang, C.H.1    Chu, Y.R.2    Ye, Y.3    Chen, X.4
  • 9
    • 73949149483 scopus 로고    scopus 로고
    • Targeted disruption of nuclear factor erythroid-derived 2-like 1 in osteoblasts reduces bone size and bone formation in mice
    • J. Kim, W. Xing, J. Wergedal, J.Y. Chan, and S. Mohan Targeted disruption of nuclear factor erythroid-derived 2-like 1 in osteoblasts reduces bone size and bone formation in mice Phys. Genomics 40 2010 100 110
    • (2010) Phys. Genomics , vol.40 , pp. 100-110
    • Kim, J.1    Xing, W.2    Wergedal, J.3    Chan, J.Y.4    Mohan, S.5
  • 10
    • 79953152999 scopus 로고    scopus 로고
    • Herp regulates Hrd1-mediated ubiquitylation in a ubiquitin-like domain-dependent manner
    • M. Kny, S. Standera, R. Hartmann-Petersen, P.M. Kloetzel, and M. Seeger Herp regulates Hrd1-mediated ubiquitylation in a ubiquitin-like domain-dependent manner J. Biol. Chem. 286 2011 5151 5156
    • (2011) J. Biol. Chem. , vol.286 , pp. 5151-5156
    • Kny, M.1    Standera, S.2    Hartmann-Petersen, R.3    Kloetzel, P.M.4    Seeger, M.5
  • 12
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • K. Kokame, K.L. Agarwala, H. Kato, and T. Miyata Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress J. Biol. Chem. 275 2000 32846 32853
    • (2000) J. Biol. Chem. , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 13
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response
    • K. Kokame, H. Kato, and T. Miyata Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response J. Biol. Chem. 276 2001 9199 9205
    • (2001) J. Biol. Chem. , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 14
    • 0039726828 scopus 로고    scopus 로고
    • The CNC basic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents. Role for Nrf1 in gamma-gcs(l) and gss expression in mouse fibroblasts
    • M. Kwong, Y.W. Kan, and J.Y. Chan The CNC basic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents. Role for Nrf1 in gamma-gcs(l) and gss expression in mouse fibroblasts J. Biol. Chem. 274 1999 37491 37498
    • (1999) J. Biol. Chem. , vol.274 , pp. 37491-37498
    • Kwong, M.1    Kan, Y.W.2    Chan, J.Y.3
  • 15
    • 84880327440 scopus 로고    scopus 로고
    • Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice
    • C.S. Lee, D.V. Ho, and J.Y. Chan Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice FEBS J. 280 2013 3609 3620
    • (2013) FEBS J. , vol.280 , pp. 3609-3620
    • Lee, C.S.1    Ho, D.V.2    Chan, J.Y.3
  • 16
  • 17
    • 84892646801 scopus 로고    scopus 로고
    • Unfolded protein response signaling and metabolic diseases
    • J. Lee, and U. Ozcan Unfolded protein response signaling and metabolic diseases J. Biol. Chem. 289 2014 1203 1211
    • (2014) J. Biol. Chem. , vol.289 , pp. 1203-1211
    • Lee, J.1    Ozcan, U.2
  • 18
    • 33750350899 scopus 로고    scopus 로고
    • Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element
    • G. Liang, T.E. Audas, Y. Li, G.P. Cockram, J.D. Dean, A.C. Martyn, K. Kokame, and R. Lu Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element Mol. Cell. Biol. 26 2006 7999 8010
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7999-8010
    • Liang, G.1    Audas, T.E.2    Li, Y.3    Cockram, G.P.4    Dean, J.D.5    Martyn, A.C.6    Kokame, K.7    Lu, R.8
  • 19
    • 1842791361 scopus 로고    scopus 로고
    • Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways
    • Y. Ma, and L.M. Hendershot Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways J. Biol. Chem. 279 2004 13792 13799
    • (2004) J. Biol. Chem. , vol.279 , pp. 13792-13799
    • Ma, Y.1    Hendershot, L.M.2
  • 21
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • P. Moi, K. Chan, I. Asunis, A. Cao, and Y.W. Kan Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region Proc. Natl. Acad. Sci. U.S.A. 91 1994 9926 9930
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 22
    • 0035951489 scopus 로고    scopus 로고
    • TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the gamma-glutamylcysteine synthetase (GCS) heavy subunit promoter
    • M.C. Myhrstad, C. Husberg, P. Murphy, O. Nordstrom, R. Blomhoff, J.O. Moskaug, and A.B. Kolsto TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the gamma-glutamylcysteine synthetase (GCS) heavy subunit promoter Biochim. et Biophys. Acta 1517 2001 212 219
    • (2001) Biochim. et Biophys. Acta , vol.1517 , pp. 212-219
    • Myhrstad, M.C.1    Husberg, C.2    Murphy, P.3    Nordstrom, O.4    Blomhoff, R.5    Moskaug, J.O.6    Kolsto, A.B.7
  • 23
    • 8544244948 scopus 로고    scopus 로고
    • The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to regulate dentin sialophosphoprotein (DSPP) gene expression during odontoblast differentiation
    • K. Narayanan, A. Ramachandran, M.C. Peterson, J. Hao, A.B. Kolsto, A.D. Friedman, and A. George The CCAAT enhancer-binding protein (C/EBP)beta and Nrf1 interact to regulate dentin sialophosphoprotein (DSPP) gene expression during odontoblast differentiation J. Biol. Chem. 279 2004 45423 45432
    • (2004) J. Biol. Chem. , vol.279 , pp. 45423-45432
    • Narayanan, K.1    Ramachandran, A.2    Peterson, M.C.3    Hao, J.4    Kolsto, A.B.5    Friedman, A.D.6    George, A.7
  • 24
    • 33645107853 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers
    • A. Nogalska, W.K. Engel, J. McFerrin, K. Kokame, H. Komano, and V. Askanas Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers J. Neurochem. 96 2006 1491 1499
    • (2006) J. Neurochem. , vol.96 , pp. 1491-1499
    • Nogalska, A.1    Engel, W.K.2    McFerrin, J.3    Kokame, K.4    Komano, H.5    Askanas, V.6
  • 25
    • 84868202074 scopus 로고    scopus 로고
    • Deficiency in the nuclear-related factor erythroid 2 transcription factor (Nrf1) leads to genetic instability
    • D.H. Oh, D. Rigas, A. Cho, and J.Y. Chan Deficiency in the nuclear-related factor erythroid 2 transcription factor (Nrf1) leads to genetic instability FEBS J. 279 2012 4121 4130
    • (2012) FEBS J. , vol.279 , pp. 4121-4130
    • Oh, D.H.1    Rigas, D.2    Cho, A.3    Chan, J.Y.4
  • 26
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Y. Okuda-Shimizu, and L.M. Hendershot Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp Mol. Cell 28 2007 544 554
    • (2007) Mol. Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 27
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • S.K. Radhakrishnan, C.S. Lee, P. Young, A. Beskow, J.Y. Chan, and R.J. Deshaies Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells Mol. Cell 38 2010 17 28
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 28
    • 84896270715 scopus 로고    scopus 로고
    • Quality control: ER-associated degradation: Protein quality control and beyond
    • A. Ruggiano, O. Foresti, and P. Carvalho 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    Foresti, O.2    Carvalho, P.3
  • 29
    • 84886615231 scopus 로고    scopus 로고
    • A deficiency of Herp, an endoplasmic reticulum stress protein, suppresses atherosclerosis in ApoE knockout mice by attenuating inflammatory responses
    • S. Shinozaki, T. Chiba, K. Kokame, T. Miyata, E. Kaneko, and K. Shimokado A deficiency of Herp, an endoplasmic reticulum stress protein, suppresses atherosclerosis in ApoE knockout mice by attenuating inflammatory responses PLoS One 8 2013 e75249
    • (2013) PLoS One , vol.8 , pp. e75249
    • Shinozaki, S.1    Chiba, T.2    Kokame, K.3    Miyata, T.4    Kaneko, E.5    Shimokado, K.6
  • 30
    • 79952844773 scopus 로고    scopus 로고
    • The unfolded protein response, degradation from endoplasmic reticulum and cancer
    • Y.C. Tsai, and A.M. Weissman The unfolded protein response, degradation from endoplasmic reticulum and cancer Genes Cancer 1 2010 764 778
    • (2010) Genes Cancer , vol.1 , pp. 764-778
    • Tsai, Y.C.1    Weissman, A.M.2
  • 31
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene
    • R. Venugopal, and A.K. Jaiswal Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene Proc. Natl. Acad. Sci. U.S.A. 93 1996 14960 14965
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 32
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • P. Walter, and D. Ron The unfolded protein response: from stress pathway to homeostatic regulation Science 334 2011 1081 1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 33
    • 84906712846 scopus 로고    scopus 로고
    • The impact of the endoplasmic reticulum protein-folding environment on cancer development
    • M. Wang, and R.J. Kaufman The impact of the endoplasmic reticulum protein-folding environment on cancer development Nat. Rev. Cancer 14 2014 581 597
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 581-597
    • Wang, M.1    Kaufman, R.J.2
  • 34
    • 84897026394 scopus 로고    scopus 로고
    • How does protein misfolding in the endoplasmic reticulum affect lipid metabolism in the liver?
    • S. Wang, and R.J. Kaufman How does protein misfolding in the endoplasmic reticulum affect lipid metabolism in the liver? Curr. Opin. Lipidol. 25 2014 125 132
    • (2014) Curr. Opin. Lipidol. , vol.25 , pp. 125-132
    • Wang, S.1    Kaufman, R.J.2
  • 35
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function
    • W. Wang, and J.Y. Chan Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function J. Biol. Chem. 281 2006 19676 19687
    • (2006) J. Biol. Chem. , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 36
    • 34547557334 scopus 로고    scopus 로고
    • Nuclear factor-E2-related factor-1 mediates ascorbic acid induction of osterix expression via interaction with antioxidant-responsive element in bone cells
    • W. Xing, A. Singgih, A. Kapoor, C.M. Alarcon, D.J. Baylink, and S. Mohan Nuclear factor-E2-related factor-1 mediates ascorbic acid induction of osterix expression via interaction with antioxidant-responsive element in bone cells J. Biol. Chem. 282 2007 22052 22061
    • (2007) J. Biol. Chem. , vol.282 , pp. 22052-22061
    • Xing, W.1    Singgih, A.2    Kapoor, A.3    Alarcon, C.M.4    Baylink, D.J.5    Mohan, S.6
  • 37
    • 15244359632 scopus 로고    scopus 로고
    • Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia
    • Z. Xu, L. Chen, L. Leung, T.S. Yen, C. Lee, and J.Y. Chan Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia Proc. Natl. Acad. Sci. U.S.A. 102 2005 4120 4125
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4120-4125
    • Xu, Z.1    Chen, L.2    Leung, L.3    Yen, T.S.4    Lee, C.5    Chan, J.Y.6
  • 38
    • 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
    • K. Yamamoto, H. Yoshida, K. Kokame, R.J. Kaufman, and K. Mori Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II J. Biochem. 136 2004 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.