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Volumn 318, Issue 19, 2012, Pages 2460-2469

Dystroglycan is associated to the disulfide isomerase ERp57

Author keywords

DG; DTT; Dystroglycan; ERp57; Fluorescence microscopy; Immunoprecipitation; NEM; Pre DG; Solid phase binding assay; SWGL

Indexed keywords

ALPHA DYSTROGLYCAN; BETA DYSTROGLYCAN; DYSTROGLYCAN; ERP57 PROTEIN; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG;

EID: 84866342604     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.07.006     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder S.J. The complexities of dystroglycan. Trends Biochem. Sci. 2001, 26:118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 2
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: from biosynthesis to pathogenesis of human disease
    • Barresi R., Campbell K.P. Dystroglycan: from biosynthesis to pathogenesis of human disease. J. Cell. Sci. 2006, 119:199-207.
    • (2006) J. Cell. Sci. , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 3
  • 4
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M, Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 1993, 122:809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 5
    • 0028122383 scopus 로고
    • Amino acid determinants that drive heparan sulfate assembly in a proteoglycan
    • Zhang L., Esko J.D. Amino acid determinants that drive heparan sulfate assembly in a proteoglycan. J. Biol. Chem. 1994, 269:19295-19299.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19295-19299
    • Zhang, L.1    Esko, J.D.2
  • 6
    • 0033976679 scopus 로고    scopus 로고
    • Biosynthesis of dystroglycan: processing of a precursor propeptide
    • Holt K.H., Crosbie R.H., Venzke D.P., Campbell K.P. Biosynthesis of dystroglycan: processing of a precursor propeptide. FEBS Lett. 2000, 468:79-83.
    • (2000) FEBS Lett. , vol.468 , pp. 79-83
    • Holt, K.H.1    Crosbie, R.H.2    Venzke, D.P.3    Campbell, K.P.4
  • 7
    • 0344009502 scopus 로고    scopus 로고
    • The effects of posttranslational processing on dystroglycan synthesis and trafficking
    • Esapa C.T., Bentham G.R., Schroder J.E., Kroger S., Blake D. The effects of posttranslational processing on dystroglycan synthesis and trafficking. FEBS Lett. 2003, 555:209-216.
    • (2003) FEBS Lett. , vol.555 , pp. 209-216
    • Esapa, C.T.1    Bentham, G.R.2    Schroder, J.E.3    Kroger, S.4    Blake, D.5
  • 8
    • 38949156757 scopus 로고    scopus 로고
    • SEA domain proteolysis determines the functional composition of dystroglycan
    • Please check the journal title, page range, year and volume number in Ref.[8], and correct if necessary.
    • Akhavan A.Please check the journal title, page range, year and volume number in Ref.[8], and correct if necessary., Crivelli S.N., Singh M., Lingappa V.R., Muschler J.L. SEA domain proteolysis determines the functional composition of dystroglycan. FASEB J. 2008, 22:612-621.
    • (2008) FASEB J. , vol.22 , pp. 612-621
    • Akhavan, A.1    Crivelli, S.N.2    Singh, M.3    Lingappa, V.R.4    Muschler, J.L.5
  • 10
    • 33750086002 scopus 로고    scopus 로고
    • Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro
    • Bozzi M., Sciandra F., Ferri L., Torreri P., Pavoni E., Petrucci T.C., Giardina B., Brancaccio A. Concerted mutation of Phe residues belonging to the beta-dystroglycan ectodomain strongly inhibits the interaction with alpha-dystroglycan in vitro. FEBS J. 2006, 273:4929-4943.
    • (2006) FEBS J. , vol.273 , pp. 4929-4943
    • Bozzi, M.1    Sciandra, F.2    Ferri, L.3    Torreri, P.4    Pavoni, E.5    Petrucci, T.C.6    Giardina, B.7    Brancaccio, A.8
  • 11
    • 68849107332 scopus 로고    scopus 로고
    • Mutagenesis at the alpha-beta interface impairs the cleavage of the dystroglycan precursor
    • Sciandra F., Bozzi M., Morlacchi S., Galtieri A., Giardina B., Brancaccio A. Mutagenesis at the alpha-beta interface impairs the cleavage of the dystroglycan precursor. FEBS J. 2009, 276:4933-4945.
    • (2009) FEBS J. , vol.276 , pp. 4933-4945
    • Sciandra, F.1    Bozzi, M.2    Morlacchi, S.3    Galtieri, A.4    Giardina, B.5    Brancaccio, A.6
  • 12
    • 33845741587 scopus 로고    scopus 로고
    • Cys669-Cys713 disulfide bridge formation is a key to dystroglycan cleavage and subunit association
    • Watanabe N., Sasaoka T., Noguchi S., Nishino I., Tanaka T. Cys669-Cys713 disulfide bridge formation is a key to dystroglycan cleavage and subunit association. Genes Cells 2007, 12:75-88.
    • (2007) Genes Cells , vol.12 , pp. 75-88
    • Watanabe, N.1    Sasaoka, T.2    Noguchi, S.3    Nishino, I.4    Tanaka, T.5
  • 13
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D., van der Wal F.J., Bulleid N.J., High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 1997, 275:86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 14
    • 33846192436 scopus 로고    scopus 로고
    • ERp57 is essential for efficient folding of glycoproteins sharing common structural domains
    • Jessop C.E., Chakravarthi S., Garbi N., Hämmerling G.J., Lovell S., Bulleid N.J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains. EMBO J. 2007, 26:28-40.
    • (2007) EMBO J. , vol.26 , pp. 28-40
    • Jessop, C.E.1    Chakravarthi, S.2    Garbi, N.3    Hämmerling, G.J.4    Lovell, S.5    Bulleid, N.J.6
  • 17
    • 0036221159 scopus 로고    scopus 로고
    • Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells
    • Coppari S., Altieri F., Ferraro A., Chichiarelli S., Eufemi M., Turano C. Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells. J. Cell. Biochem. 2002, 85:325-333.
    • (2002) J. Cell. Biochem. , vol.85 , pp. 325-333
    • Coppari, S.1    Altieri, F.2    Ferraro, A.3    Chichiarelli, S.4    Eufemi, M.5    Turano, C.6
  • 19
    • 2442624604 scopus 로고    scopus 로고
    • Ribozyme knockdown functionally links a 1,25(OH)2D3 membrane binding protein (1,25D3-MARRS) and phosphate uptake in intestinal cells
    • Nemere I., Farach-Carson M.C., Rohe B., Sterling T.M., Norman A.W., Boyan B.D., Safford S.E. Ribozyme knockdown functionally links a 1,25(OH)2D3 membrane binding protein (1,25D3-MARRS) and phosphate uptake in intestinal cells. Proc. Natl. Acad. Sci. USA 2004, 101:7392-7397.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7392-7397
    • Nemere, I.1    Farach-Carson, M.C.2    Rohe, B.3    Sterling, T.M.4    Norman, A.W.5    Boyan, B.D.6    Safford, S.E.7
  • 21
    • 84864120972 scopus 로고    scopus 로고
    • Insertion of a myc-tag within a-dystroglycan domains improves its biochemical and microscopic detection
    • DOI: 10.1186/1471-2091-13-14
    • Morlacchi S., Sciandra F., Bigotti M.G., Bozzi M., Hubner W., Galtieri A., Giardina B., Brancaccio A., Insertion of a myc-tag within a-dystroglycan domains improves its biochemical and microscopic detection, BMC Biochemistry, Vol 13(1), DOI: 10.1186/1471-2091-13-14, 2012.
    • (2012) BMC Biochemistry , vol.13 , Issue.1
    • Morlacchi, S.1    Sciandra, F.2    Bigotti, M.G.3    Bozzi, M.4    Hubner, W.5    Galtieri, A.6    Giardina, B.7    Brancaccio, A.8
  • 23
    • 0031761254 scopus 로고    scopus 로고
    • A single disulfide bridge (Cys182-Cys264) is crucial for alpha-dystroglycan N-terminal domain stability
    • Brancaccio A., Jenö P., Engel J. A single disulfide bridge (Cys182-Cys264) is crucial for alpha-dystroglycan N-terminal domain stability. Ann. N. Y. Acad. Sci. 1998, 857:228-231.
    • (1998) Ann. N. Y. Acad. Sci. , vol.857 , pp. 228-231
    • Brancaccio, A.1    Jenö, P.2    Engel, J.3
  • 26
    • 0030916837 scopus 로고    scopus 로고
    • The N-terminal region of alpha-dystroglycan is an autonomous globular domain
    • Brancaccio A., Schulthess T., Gesemann M., Engel J. The N-terminal region of alpha-dystroglycan is an autonomous globular domain. Eur. J. Biochem. 1997, 246:166-172.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 166-172
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 27
    • 59049105293 scopus 로고    scopus 로고
    • Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin
    • Jessop C.E., Tavender T.J., Watkins R.H., Chambers J.E., Bulleid N.J. Substrate specificity of the oxidoreductase ERp57 is determined primarily by its interaction with calnexin and calreticulin. J. Biol. Chem. 2009, 284:2194-2202.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2194-2202
    • Jessop, C.E.1    Tavender, T.J.2    Watkins, R.H.3    Chambers, J.E.4    Bulleid, N.J.5
  • 29
    • 0036842559 scopus 로고    scopus 로고
    • Formation and transfer of disulfide bonds in living cells
    • Sevier C.S., Kaiser C.A. Formation and transfer of disulfide bonds in living cells. Nat. Rev. Mol. Cell Biol. 2002, 3:836-847.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 836-847
    • Sevier, C.S.1    Kaiser, C.A.2
  • 30
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted folding
    • Walker K.W., Gilbert H.F. Scanning and escape during protein-disulfide isomerase-assisted folding. J. Biol. Chem. 1997, 272:8845-8848.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 31
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper D.R., Wearsch P.A., Cresswell P. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J. 2005, 24:3613-3623.
    • (2005) EMBO J. , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 32
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg P.J. Disulfide bonds as switches for protein function. Trends Biochem. Sci. 2003, 28:210-214.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 33
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan P.A., Gibbins J.M. Extracellular disulfide exchange and the regulation of cellular function. Antioxid. Redox Signal. 2006, 8:312-324.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 35
    • 0034737776 scopus 로고    scopus 로고
    • Physical proximity and functional association of glycoprotein 1ba and protein disulfide isomerase on the platelet plasma membrane
    • Burgess J.K., Hotchkiss K.A., Suter C., Dudman N.P.B., Szollosi J., Chesterman C.N., Chong B.H., Hogg P.J. Physical proximity and functional association of glycoprotein 1ba and protein disulfide isomerase on the platelet plasma membrane. J. Biol. Chem. 2000, 275:9758-9766.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9758-9766
    • Burgess, J.K.1    Hotchkiss, K.A.2    Suter, C.3    Dudman, N.P.B.4    Szollosi, J.5    Chesterman, C.N.6    Chong, B.H.7    Hogg, P.J.8


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