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Volumn 340, Issue 2, 2006, Pages 617-624

ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulin

Author keywords

Chaperone; Endoplasmic reticulum; ERp29; Secretion; Thyroglobulin

Indexed keywords

CYSTEINE; GLUTAMINE; PROTEIN; PROTEIN ERP29; THYROGLOBULIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 29644440061     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.12.052     Document Type: Article
Times cited : (52)

References (28)
  • 2
    • 0030792377 scopus 로고    scopus 로고
    • Combination of direct DNA sequencing with degenerate primer-mediated PCR and 5′-/3′-RACE to screen novel cDNA sequences
    • C. Fang, S. Mkrtchian, and M. Ingelman-Sundberg Combination of direct DNA sequencing with degenerate primer-mediated PCR and 5′-/3′-RACE to screen novel cDNA sequences Biotechniques 23 1997 52, 54, 56, 58
    • (1997) Biotechniques , vol.23
    • Fang, C.1    Mkrtchian, S.2    Ingelman-Sundberg, M.3
  • 3
    • 0031054441 scopus 로고    scopus 로고
    • Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum
    • J. Demmer, C. Zhou, and M.J. Hubbard Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum FEBS Lett. 402 1997 145 150
    • (1997) FEBS Lett. , vol.402 , pp. 145-150
    • Demmer, J.1    Zhou, C.2    Hubbard, M.J.3
  • 4
    • 0032146759 scopus 로고    scopus 로고
    • ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif
    • D.M. Ferrari, P. Nguyen Van, H.D. Kratzin, and H.D. Soling ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif Eur. J. Biochem. 255 1998 570 579
    • (1998) Eur. J. Biochem. , vol.255 , pp. 570-579
    • Ferrari, D.M.1    Nguyen Van, P.2    Kratzin, H.D.3    Soling, H.D.4
  • 5
    • 0037138390 scopus 로고    scopus 로고
    • Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29
    • E. Sargsyan, M. Baryshev, M. Backlund, A. Sharipo, and S. Mkrtchian Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29 Gene 285 2002 127 139
    • (2002) Gene , vol.285 , pp. 127-139
    • Sargsyan, E.1    Baryshev, M.2    Backlund, M.3    Sharipo, A.4    Mkrtchian, S.5
  • 6
    • 0034108939 scopus 로고    scopus 로고
    • Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis
    • M.J. Hubbard, N.J. McHugh, and D.L. Carne Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis Eur. J. Biochem. 267 2000 1945 1957
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1945-1957
    • Hubbard, M.J.1    McHugh, N.J.2    Carne, D.L.3
  • 7
    • 0034989106 scopus 로고    scopus 로고
    • Thioredoxin Fold as Homodimerization Module in the Putative Chaperone ERp29. NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer
    • E. Liepinsh, M. Baryshev, A. Sharipo, M. Ingelman-Sundberg, G. Otting, and S. Mkrtchian Thioredoxin Fold as Homodimerization Module in the Putative Chaperone ERp29. NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer Structure 9 2001 457 471
    • (2001) Structure , vol.9 , pp. 457-471
    • Liepinsh, E.1    Baryshev, M.2    Sharipo, A.3    Ingelman-Sundberg, M.4    Otting, G.5    Mkrtchian, S.6
  • 8
    • 9144252641 scopus 로고    scopus 로고
    • Purification and biochemical characterization of native ERp29 from rat liver
    • M.J. Hubbard, J.E. Mangum, and N.J. McHugh Purification and biochemical characterization of native ERp29 from rat liver Biochem. J. 383 2004 589 597
    • (2004) Biochem. J. , vol.383 , pp. 589-597
    • Hubbard, M.J.1    Mangum, J.E.2    McHugh, N.J.3
  • 10
    • 0034524031 scopus 로고    scopus 로고
    • Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe
    • J. Sen, J.S. Goltz, M. Konsolaki, T. Schupbach, and D. Stein Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe Development 127 2000 5541 5550
    • (2000) Development , vol.127 , pp. 5541-5550
    • Sen, J.1    Goltz, J.S.2    Konsolaki, M.3    Schupbach, T.4    Stein, D.5
  • 11
    • 0037053397 scopus 로고    scopus 로고
    • Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex
    • E. Sargsyan, M. Baryshev, L. Szekely, A. Sharipo, and S. Mkrtchian Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex J. Biol. Chem. 277 2002 17009 17015
    • (2002) J. Biol. Chem. , vol.277 , pp. 17009-17015
    • Sargsyan, E.1    Baryshev, M.2    Szekely, L.3    Sharipo, A.4    Mkrtchian, S.5
  • 12
    • 0030981967 scopus 로고    scopus 로고
    • Intracellular protein transport to the thyrocyte plasma membrane: Potential implications for thyroid physiology
    • P. Arvan, P.S. Kim, R. Kuliawat, D. Prabakaran, Z. Muresan, S.E. Yoo, and S. Abu Hossain Intracellular protein transport to the thyrocyte plasma membrane: potential implications for thyroid physiology Thyroid 7 1997 89 105
    • (1997) Thyroid , vol.7 , pp. 89-105
    • Arvan, P.1    Kim, P.S.2    Kuliawat, R.3    Prabakaran, D.4    Muresan, Z.5    Yoo, S.E.6    Abu Hossain, S.7
  • 13
    • 0034625576 scopus 로고    scopus 로고
    • TSH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells
    • O.Y. Kwon, S. Park, W. Lee, K.H. You, H. Kim, and M. Shong TSH regulates a gene expression encoding ERp29, an endoplasmic reticulum stress protein, in the thyrocytes of FRTL-5 cells FEBS Lett. 475 2000 27 30
    • (2000) FEBS Lett. , vol.475 , pp. 27-30
    • Kwon, O.Y.1    Park, S.2    Lee, W.3    You, K.H.4    Kim, H.5    Shong, M.6
  • 14
    • 6044255043 scopus 로고    scopus 로고
    • The physiological unfolded protein response in the thyroid epithelial cells
    • E. Sargsyan, M. Baryshev, and S. Mkrtchian The physiological unfolded protein response in the thyroid epithelial cells Biochem. Biophys. Res. Commun. 322 2004 570 576
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 570-576
    • Sargsyan, E.1    Baryshev, M.2    Mkrtchian, S.3
  • 15
    • 3042771829 scopus 로고    scopus 로고
    • Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism
    • M. Baryshev, E. Sargsyan, G. Wallin, A. Lejnieks, S. Furudate, A. Hishinuma, and S. Mkrtchian Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism J. Mol. Endocrinol. 32 2004 903 920
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 903-920
    • Baryshev, M.1    Sargsyan, E.2    Wallin, G.3    Lejnieks, A.4    Furudate, S.5    Hishinuma, A.6    Mkrtchian, S.7
  • 16
    • 0242497806 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein
    • Q. Ma, C. Guo, K. Barnewitz, G.M. Sheldrick, H.D. Soling, I. Uson, and D.M. Ferrari Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein J. Biol. Chem. 278 2003 44600 44607
    • (2003) J. Biol. Chem. , vol.278 , pp. 44600-44607
    • Ma, Q.1    Guo, C.2    Barnewitz, K.3    Sheldrick, G.M.4    Soling, H.D.5    Uson, I.6    Ferrari, D.M.7
  • 17
    • 0025362658 scopus 로고
    • Recycling of proteins from the Golgi compartment to the ER in yeast
    • N. Dean, and H.R. Pelham Recycling of proteins from the Golgi compartment to the ER in yeast J. Cell Biol. 111 1990 369 377
    • (1990) J. Cell Biol. , vol.111 , pp. 369-377
    • Dean, N.1    Pelham, H.R.2
  • 18
    • 0025866855 scopus 로고
    • Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP
    • C.K. Suzuki, J.S. Bonifacino, A.Y. Lin, M.M. Davis, and R.D. Klausner Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP J. Cell Biol. 114 1991 189 205
    • (1991) J. Cell Biol. , vol.114 , pp. 189-205
    • Suzuki, C.K.1    Bonifacino, J.S.2    Lin, A.Y.3    Davis, M.M.4    Klausner, R.D.5
  • 19
    • 4544371124 scopus 로고    scopus 로고
    • Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure
    • K. Barnewitz, C. Guo, M. Sevvana, Q. Ma, G.M. Sheldrick, H.D. Soling, and D.M. Ferrari Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure J. Biol. Chem. 279 2004 39829 39837
    • (2004) J. Biol. Chem. , vol.279 , pp. 39829-39837
    • Barnewitz, K.1    Guo, C.2    Sevvana, M.3    Ma, Q.4    Sheldrick, G.M.5    Soling, H.D.6    Ferrari, D.M.7
  • 20
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • L. Ellgaard, and A. Helenius Quality control in the endoplasmic reticulum Nat. Rev. Mol. Cell Biol. 4 2003 181 191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 21
    • 0030666195 scopus 로고    scopus 로고
    • Thyroglobulin transport along the secretory pathway. Investigation of the role of molecular chaperone, GRP94, in protein export from the endoplasmic reticulum
    • Z. Muresan, and P. Arvan Thyroglobulin transport along the secretory pathway. Investigation of the role of molecular chaperone, GRP94, in protein export from the endoplasmic reticulum J. Biol. Chem. 272 1997 26095 26102
    • (1997) J. Biol. Chem. , vol.272 , pp. 26095-26102
    • Muresan, Z.1    Arvan, P.2
  • 22
    • 0032230314 scopus 로고    scopus 로고
    • Enhanced binding to the molecular chaperone BiP slows thyroglobulin export from the endoplasmic reticulum
    • Z. Muresan, and P. Arvan Enhanced binding to the molecular chaperone BiP slows thyroglobulin export from the endoplasmic reticulum Mol. Endocrinol. 12 1998 458 467
    • (1998) Mol. Endocrinol. , vol.12 , pp. 458-467
    • Muresan, Z.1    Arvan, P.2
  • 23
    • 0030939508 scopus 로고    scopus 로고
    • Enhancement of protein secretion in Saccharomyces cerevisiae by overproduction of Sso protein, a late-acting component of the secretory machinery
    • L. Ruohonen, J. Toikkanen, V. Tieaho, M. Outola, H. Soderlund, and S. Keranen Enhancement of protein secretion in Saccharomyces cerevisiae by overproduction of Sso protein, a late-acting component of the secretory machinery Yeast 13 1997 337 351
    • (1997) Yeast , vol.13 , pp. 337-351
    • Ruohonen, L.1    Toikkanen, J.2    Tieaho, V.3    Outola, M.4    Soderlund, H.5    Keranen, S.6
  • 24
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells
    • S.H. Chung, Y. Takai, and R.W. Holz Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells J. Biol. Chem. 270 1995 16714 16718
    • (1995) J. Biol. Chem. , vol.270 , pp. 16714-16718
    • Chung, S.H.1    Takai, Y.2    Holz, R.W.3
  • 25
    • 10644247772 scopus 로고    scopus 로고
    • Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations
    • S.H. Liu, W.I. Chou, C.C. Sheu, and M.D. Chang Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations Biochem. Biophys. Res. Commun. 326 2005 817 824
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 817-824
    • Liu, S.H.1    Chou, W.I.2    Sheu, C.C.3    Chang, M.D.4
  • 26
    • 29644438156 scopus 로고    scopus 로고
    • Biophysical characterization of ERp29: Evidence for a key structural role of cysteine-125
    • V.M. Hermann, J.F. Cutfield, and M.J. Hubbard Biophysical characterization of ERp29: evidence for a key structural role of cysteine-125 J. Biol. Chem. 2004
    • (2004) J. Biol. Chem.
    • Hermann, V.M.1    Cutfield, J.F.2    Hubbard, M.J.3
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11 1991 281 296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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