메뉴 건너뛰기




Volumn 41, Issue 7, 2014, Pages 357-368

The E3 ubiquitin ligase gp78 protects against ER stress in zebrafish liver

Author keywords

Cholesterol; ERAD; Gp78 AMFR; Lipogenesis; UPR; Zebrafish

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN; PROTEIN GP78; STEROL REGULATORY ELEMENT BINDING PROTEIN; TUNICAMYCIN; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UBIQUITIN PROTEIN LIGASE;

EID: 84904719533     PISSN: 16738527     EISSN: 18735533     Source Type: Journal    
DOI: 10.1016/j.jgg.2014.05.005     Document Type: Article
Times cited : (16)

References (49)
  • 2
    • 70549109093 scopus 로고    scopus 로고
    • Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1
    • Ballar P., Ors A.U., Yang H., Fang S. Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1. Int. J. Biochem. Cell Biol. 2010, 42:167-173.
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 167-173
    • Ballar, P.1    Ors, A.U.2    Yang, H.3    Fang, S.4
  • 3
    • 33845917801 scopus 로고    scopus 로고
    • The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation
    • Ballar P., Shen Y., Yang H., Fang S. The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation. J. Biol. Chem. 2006, 281:35359-35368.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35359-35368
    • Ballar, P.1    Shen, Y.2    Yang, H.3    Fang, S.4
  • 5
    • 79960471805 scopus 로고    scopus 로고
    • Development of a transgenic zebrafish model expressing GFP in the notochord, somite and liver directed by the hfe2 gene promoter
    • Bian Y.H., Xu C., Li J., Xu J., Zhang H., Du S.J. Development of a transgenic zebrafish model expressing GFP in the notochord, somite and liver directed by the hfe2 gene promoter. Transgenic Res. 2011, 20:787-798.
    • (2011) Transgenic Res. , vol.20 , pp. 787-798
    • Bian, Y.H.1    Xu, C.2    Li, J.3    Xu, J.4    Zhang, H.5    Du, S.J.6
  • 6
    • 84866558646 scopus 로고    scopus 로고
    • Gp78: a multifaceted ubiquitin ligase that integrates a unique protein degradation pathway from the endoplasmic reticulum
    • Chen Z., Du S., Fang S. gp78: a multifaceted ubiquitin ligase that integrates a unique protein degradation pathway from the endoplasmic reticulum. Curr. Protein Pept. Sci. 2012, 13:414-424.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 414-424
    • Chen, Z.1    Du, S.2    Fang, S.3
  • 7
    • 79960740818 scopus 로고    scopus 로고
    • Activating transcription factor 6 plays protective and pathological roles in steatosis due to endoplasmic reticulum stress in zebrafish
    • Cinaroglu A., Gao C., Imrie D., Sadler K.C. Activating transcription factor 6 plays protective and pathological roles in steatosis due to endoplasmic reticulum stress in zebrafish. Hepatology 2011, 54:495-508.
    • (2011) Hepatology , vol.54 , pp. 495-508
    • Cinaroglu, A.1    Gao, C.2    Imrie, D.3    Sadler, K.C.4
  • 9
    • 0035083121 scopus 로고    scopus 로고
    • Gli2 mediation of hedgehog signals in slow muscle induction in zebrafish
    • Du S.J., Dienhart M. Gli2 mediation of hedgehog signals in slow muscle induction in zebrafish. Differentiation 2001, 67:84-91.
    • (2001) Differentiation , vol.67 , pp. 84-91
    • Du, S.J.1    Dienhart, M.2
  • 10
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S., Ferrone M., Yang C., Jensen J.P., Tiwari S., Weissman A.M. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 2001, 98:14422-14427.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 11
    • 79956050306 scopus 로고    scopus 로고
    • Ubiquitination regulates the assembly of VLDL in HepG2 cells and is the committing step of the apoB-100 ERAD pathway
    • Fisher E.A., Khanna N.A., McLeod R.S. Ubiquitination regulates the assembly of VLDL in HepG2 cells and is the committing step of the apoB-100 ERAD pathway. J. Lipid Res. 2011, 52:1170-1180.
    • (2011) J. Lipid Res. , vol.52 , pp. 1170-1180
    • Fisher, E.A.1    Khanna, N.A.2    McLeod, R.S.3
  • 12
    • 79955839745 scopus 로고    scopus 로고
    • Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release
    • Fu M., Li L., Albrecht T., Johnson J.D., Kojic L.D., Nabi I.R. Autocrine motility factor/phosphoglucose isomerase regulates ER stress and cell death through control of ER calcium release. Cell Death Differ. 2011, 18:1057-1070.
    • (2011) Cell Death Differ. , vol.18 , pp. 1057-1070
    • Fu, M.1    Li, L.2    Albrecht, T.3    Johnson, J.D.4    Kojic, L.D.5    Nabi, I.R.6
  • 14
    • 77950556316 scopus 로고    scopus 로고
    • A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase
    • Joshi B., Li L., Nabi I.R. A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase. J. Biol. Chem. 2010, 285:8830-8839.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8830-8839
    • Joshi, B.1    Li, L.2    Nabi, I.R.3
  • 15
    • 66449137379 scopus 로고    scopus 로고
    • GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice
    • Kammoun H.L., Chabanon H., Hainault I., Luquet S., Magnan C., Koike T., Ferre P., Foufelle F. GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice. J. Clin. Invest. 2009, 119:1201-1215.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1201-1215
    • Kammoun, H.L.1    Chabanon, H.2    Hainault, I.3    Luquet, S.4    Magnan, C.5    Koike, T.6    Ferre, P.7    Foufelle, F.8
  • 16
    • 78149241047 scopus 로고    scopus 로고
    • Liver cytochrome P450 3A ubiquitination invivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: physiological and pharmacological relevance
    • Kim S.M., Acharya P., Engel J.C., Correia M.A. Liver cytochrome P450 3A ubiquitination invivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: physiological and pharmacological relevance. J. Biol. Chem. 2010, 285:35866-35877.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35866-35877
    • Kim, S.M.1    Acharya, P.2    Engel, J.C.3    Correia, M.A.4
  • 17
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Kostova Z., Tsai Y.C., Weissman A.M. Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin. Cell Dev. Biol. 2007, 18:770-779.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 18
    • 83055164361 scopus 로고    scopus 로고
    • Smyd1b_tv1, a key regulator of sarcomere assembly, is localized on the M-line of skeletal muscle fibers
    • Li H., Xu J., Bian Y.H., Rotllant P., Shen T., Chu W., Zhang J., Schneider M., Du S.J. Smyd1b_tv1, a key regulator of sarcomere assembly, is localized on the M-line of skeletal muscle fibers. PLoS ONE 2011, 6:e28524.
    • (2011) PLoS ONE , vol.6
    • Li, H.1    Xu, J.2    Bian, Y.H.3    Rotllant, P.4    Shen, T.5    Chu, W.6    Zhang, J.7    Schneider, M.8    Du, S.J.9
  • 19
    • 62649096662 scopus 로고    scopus 로고
    • Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
    • Li W., Tu D., Li L., Wollert T., Ghirlando R., Brunger A.T., Ye Y. Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc. Natl. Acad. Sci. USA 2009, 106:3722-3727.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3722-3727
    • Li, W.1    Tu, D.2    Li, L.3    Wollert, T.4    Ghirlando, R.5    Brunger, A.T.6    Ye, Y.7
  • 20
    • 34247186766 scopus 로고    scopus 로고
    • Animal models of human disease: zebrafish swim into view
    • Lieschke G.J., Currie P.D. Animal models of human disease: zebrafish swim into view. Nat. Rev. Genet. 2007, 8:353-367.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 353-367
    • Lieschke, G.J.1    Currie, P.D.2
  • 21
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • Liu T.F., Tang J.J., Li P.S., Shen Y., Li J.G., Miao H.H., Li B.L., Song B.L. Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis. Cell Metab. 2012, 16:213-225.
    • (2012) Cell Metab. , vol.16 , pp. 213-225
    • Liu, T.F.1    Tang, J.J.2    Li, P.S.3    Shen, Y.4    Li, J.G.5    Miao, H.H.6    Li, B.L.7    Song, B.L.8
  • 22
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 2007, 18:716-731.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 23
    • 77957189436 scopus 로고    scopus 로고
    • ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum
    • Mehnert M., Sommer T., Jarosch E. ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 2010, 32:905-913.
    • (2010) Bioessays , vol.32 , pp. 905-913
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 25
    • 0033780376 scopus 로고    scopus 로고
    • Effective targeted gene 'knockdown' in zebrafish
    • Nasevicius A., Ekker S.C. Effective targeted gene 'knockdown' in zebrafish. Nat. Genet. 2000, 26:216-220.
    • (2000) Nat. Genet. , vol.26 , pp. 216-220
    • Nasevicius, A.1    Ekker, S.C.2
  • 26
    • 84864269699 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in nonalcoholic Fatty liver disease
    • Pagliassotti M.J. Endoplasmic reticulum stress in nonalcoholic Fatty liver disease. Annu. Rev. Nutr. 2012, 32:17-33.
    • (2012) Annu. Rev. Nutr. , vol.32 , pp. 17-33
    • Pagliassotti, M.J.1
  • 27
    • 61949349873 scopus 로고    scopus 로고
    • Hepatic steatosis in response to acute alcohol exposure in zebrafish requires sterol regulatory element binding protein activation
    • Passeri M.J., Cinaroglu A., Gao C., Sadler K.C. Hepatic steatosis in response to acute alcohol exposure in zebrafish requires sterol regulatory element binding protein activation. Hepatology 2009, 49:443-452.
    • (2009) Hepatology , vol.49 , pp. 443-452
    • Passeri, M.J.1    Cinaroglu, A.2    Gao, C.3    Sadler, K.C.4
  • 28
    • 79952774815 scopus 로고    scopus 로고
    • CHIP and gp78-mediated ubiquitination of CYP3A4: implications for the pharmacology of anticancer agents
    • Peer C.J., Sissung T.M., Figg W.D. CHIP and gp78-mediated ubiquitination of CYP3A4: implications for the pharmacology of anticancer agents. Cancer Biol. Ther. 2011, 11:549-551.
    • (2011) Cancer Biol. Ther. , vol.11 , pp. 549-551
    • Peer, C.J.1    Sissung, T.M.2    Figg, W.D.3
  • 29
    • 0034667598 scopus 로고    scopus 로고
    • Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction
    • Ponting C.P. Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. Biochem. J. 2000, 351(Pt 2):527-535.
    • (2000) Biochem. J. , vol.351 , Issue.PART 2 , pp. 527-535
    • Ponting, C.P.1
  • 30
    • 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
  • 31
    • 34548440339 scopus 로고    scopus 로고
    • ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD anddevelopmental growth in Caenorhabditis elegans
    • Sasagawa Y., Yamanaka K., Ogura T. ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play important roles in ERAD anddevelopmental growth in Caenorhabditis elegans. Genes Cells 2007, 12:1063-1073.
    • (2007) Genes Cells , vol.12 , pp. 1063-1073
    • Sasagawa, Y.1    Yamanaka, K.2    Ogura, T.3
  • 32
    • 33845451008 scopus 로고    scopus 로고
    • ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates
    • Shen Y., Ballar P., Apostolou A., Doong H., Fang S. ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates. Biochem. Biophys. Res. Commun. 2007, 352:919-924.
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 919-924
    • Shen, Y.1    Ballar, P.2    Apostolou, A.3    Doong, H.4    Fang, S.5
  • 33
    • 33748792529 scopus 로고    scopus 로고
    • Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin
    • Shen Y., Ballar P., Fang S. Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin. Biochem. Biophys. Res. Commun. 2006, 349:1285-1293.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1285-1293
    • Shen, Y.1    Ballar, P.2    Fang, S.3
  • 35
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
    • Song B.L., Sever N., DeBose-Boyd R.A. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell 2005, 19:829-840.
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    DeBose-Boyd, R.A.3
  • 36
    • 33644542409 scopus 로고    scopus 로고
    • SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos
    • Tan X., Rotllant J., Li H., De Deyne P., Du S.J. SmyD1, a histone methyltransferase, is required for myofibril organization and muscle contraction in zebrafish embryos. Proc. Natl. Acad. Sci. USA 2006, 103:2713-2718.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2713-2718
    • Tan, X.1    Rotllant, J.2    Li, H.3    De Deyne, P.4    Du, S.J.5
  • 37
    • 79960739850 scopus 로고    scopus 로고
    • Lack of de novo phosphatidylinositol synthesis leads to endoplasmic reticulum stress and hepatic steatosis in cdipt-deficient zebrafish
    • Thakur P.C., Stuckenholz C., Rivera M.R., Davison J.M., Yao J.K., Amsterdam A., Sadler K.C., Bahary N. Lack of de novo phosphatidylinositol synthesis leads to endoplasmic reticulum stress and hepatic steatosis in cdipt-deficient zebrafish. Hepatology 2011, 54:452-462.
    • (2011) Hepatology , vol.54 , pp. 452-462
    • Thakur, P.C.1    Stuckenholz, C.2    Rivera, M.R.3    Davison, J.M.4    Yao, J.K.5    Amsterdam, A.6    Sadler, K.C.7    Bahary, N.8
  • 38
    • 0035844139 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)
    • Tiwari S., Weissman A.M. Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J. Biol. Chem. 2001, 276:16193-16200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16193-16200
    • Tiwari, S.1    Weissman, A.M.2
  • 40
    • 33750433896 scopus 로고    scopus 로고
    • Functional dissection of the Tol2 transposable element identified the minimal cis-sequence and a highly repetitive sequence in the subterminal region essential for transposition
    • Urasaki A., Morvan G., Kawakami K. Functional dissection of the Tol2 transposable element identified the minimal cis-sequence and a highly repetitive sequence in the subterminal region essential for transposition. Genetics 2006, 174:639-649.
    • (2006) Genetics , vol.174 , pp. 639-649
    • Urasaki, A.1    Morvan, G.2    Kawakami, K.3
  • 41
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 2008, 9:944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 42
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P., Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334:1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 43
    • 79953219048 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteasomal degradation of human liver cytochrome P450 2E1: identification of sites targeted for phosphorylation and ubiquitination
    • Wang Y., Guan S., Acharya P., Koop D.R., Liu Y., Liao M., Burlingame A.L., Correia M.A. Ubiquitin-dependent proteasomal degradation of human liver cytochrome P450 2E1: identification of sites targeted for phosphorylation and ubiquitination. J. Biol. Chem. 2011, 286:9443-9456.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9443-9456
    • Wang, Y.1    Guan, S.2    Acharya, P.3    Koop, D.R.4    Liu, Y.5    Liao, M.6    Burlingame, A.L.7    Correia, M.A.8
  • 44
    • 84879410743 scopus 로고    scopus 로고
    • TALEN or Cas9-rapid, efficient and specific choices for genome modifications
    • Wei C., Liu J., Yu Z., Zhang B., Gao G., Jiao R. TALEN or Cas9-rapid, efficient and specific choices for genome modifications. J. Genet. Genomics 2013, 40:281-289.
    • (2013) J. Genet. Genomics , vol.40 , pp. 281-289
    • Wei, C.1    Liu, J.2    Yu, Z.3    Zhang, B.4    Gao, G.5    Jiao, R.6
  • 46
    • 84862801738 scopus 로고    scopus 로고
    • Functional analysis of slow myosin heavy chain 1 and myomesin-3 in sarcomere organization in zebrafish embryonic slow muscles
    • Xu J., Gao J., Li J., Xue L., Clark K.J., Ekker S.C., Du S.J. Functional analysis of slow myosin heavy chain 1 and myomesin-3 in sarcomere organization in zebrafish embryonic slow muscles. J. Genet. Genomics 2012, 39:69-80.
    • (2012) J. Genet. Genomics , vol.39 , pp. 69-80
    • Xu, J.1    Gao, J.2    Li, J.3    Xue, L.4    Clark, K.J.5    Ekker, S.C.6    Du, S.J.7
  • 48
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang H., Liu C., Zhong Y., Luo S., Monteiro M.J., Fang S. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS ONE 2010, 5:e8905.
    • (2010) PLoS ONE , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 49
    • 70350701842 scopus 로고    scopus 로고
    • Gp78, an ER associated E3, promotes SOD1 and ataxin-3 degradation
    • Ying Z., Wang H., Fan H., Zhu X., Zhou J., Fei E., Wang G. Gp78, an ER associated E3, promotes SOD1 and ataxin-3 degradation. Hum. Mol. Genet. 2009, 18:4268-4281.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4268-4281
    • Ying, Z.1    Wang, H.2    Fan, H.3    Zhu, X.4    Zhou, J.5    Fei, E.6    Wang, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.