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Volumn 122, Issue 4, 1997, Pages 834-842

Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease

Author keywords

Active site; Cysteine protease; Endoplasmic reticulum; Retention signal; Site directed mutagenesis

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; ALANINE; COMPLEMENTARY DNA; CYSTEINE; CYSTEINE PROTEINASE; DYFLOS; MICROSOME ENZYME; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT ENZYME; SERINE; SIGNAL PEPTIDE;

EID: 0030699084     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021830     Document Type: Article
Times cited : (39)

References (34)
  • 1
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S.M. and Helenius, A. (1989) Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 2
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman, J.E. (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59, 591-601
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 3
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 4
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R.D. and Sitia, R. (1990) Protein degradation in the endoplasmic reticulum. Cell 62, 611-614
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 6
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase C-α family from rat liver endoplasmic reticulum
    • Urade, R., Nasu, M., Moriyama, T., Wada, K., and Kito, M. (1992) Protein degradation by the phosphoinositide-specific phospholipase C-α family from rat liver endoplasmic reticulum. J. Biol. Chem. 267, 15152-15159
    • (1992) J. Biol. Chem. , vol.267 , pp. 15152-15159
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 7
    • 0026673355 scopus 로고
    • Inhibition by acidic phospholipids of protein degradation by ER-60 protease, a novel cysteine protease, of endoplasmic reticulum
    • Urade, R. and Kito, M. (1992) Inhibition by acidic phospholipids of protein degradation by ER-60 protease, a novel cysteine protease, of endoplasmic reticulum. FEBS Lett. 312, 83-86
    • (1992) FEBS Lett. , vol.312 , pp. 83-86
    • Urade, R.1    Kito, M.2
  • 8
    • 0022547428 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum
    • Lewis, M.J., Mazzarella, R.A., and Green, M. (1986) Structure and assembly of the endoplasmic reticulum: Biosynthesis and intracellular sorting of ERp61, ERp59, and ERp49, three protein components of murine endoplasmic reticulum. Arch. Biochem. Biophys. 245, 389-403
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 389-403
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 9
    • 0025699165 scopus 로고
    • HIP-70: An isoform of phosphoinositol-specific phospholipase C-α
    • Mobbs, C.V., Fink, G., and Pfaff, D.W. (1990) HIP-70: An isoform of phosphoinositol-specific phospholipase C-α. Science 249, 566-567
    • (1990) Science , vol.249 , pp. 566-567
    • Mobbs, C.V.1    Fink, G.2    Pfaff, D.W.3
  • 10
    • 0025830169 scopus 로고
    • Purification and characterization of a new isozyme of thiol: Protein-disulfide oxidoreductase from rat hepatic microsomes
    • Srivastava, S.P., Chen, N., Liu, Y., and Holtzman, J.L. (1991) Purification and characterization of a new isozyme of thiol: protein-disulfide oxidoreductase from rat hepatic microsomes. J. Biol. Chem. 266, 20337-20344
    • (1991) J. Biol. Chem. , vol.266 , pp. 20337-20344
    • Srivastava, S.P.1    Chen, N.2    Liu, Y.3    Holtzman, J.L.4
  • 11
    • 0028223563 scopus 로고
    • ERp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity
    • Mazzarella, R.A., Marcus, N., Haugejorden, S.M., Balcarek, J.M., Baldassare, J.J., Roy, B., Li, L., Lee, A.S., and Green, M. (1994) ERp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. Arch. Biochem. Biophys. 308, 454-460
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 454-460
    • Mazzarella, R.A.1    Marcus, N.2    Haugejorden, S.M.3    Balcarek, J.M.4    Baldassare, J.J.5    Roy, B.6    Li, L.7    Lee, A.S.8    Green, M.9
  • 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., and High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 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
    • 0029074071 scopus 로고
    • A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum
    • Otsu, M., Urade, R., Kito, M., Omura, F., and Kikuchi, M. (1995) A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum. J. Biol. Chem. 270, 14958-14961
    • (1995) J. Biol. Chem. , vol.270 , pp. 14958-14961
    • Otsu, M.1    Urade, R.2    Kito, M.3    Omura, F.4    Kikuchi, M.5
  • 15
    • 85008070372 scopus 로고
    • Role of novel microsomal cysteine proteases
    • Kito, M. and Urade, R. (1995) Role of novel microsomal cysteine proteases. Proc. Jpn. Acad. 71B, 189-192
    • (1995) Proc. Jpn. Acad. , vol.71 B , pp. 189-192
    • Kito, M.1    Urade, R.2
  • 16
  • 17
    • 0027501384 scopus 로고
    • Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum
    • Urade, R., Takenaka, Y., and Kito, M. (1995) Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum. J. Biol. Chem. 268, 22004-22009
    • (1995) J. Biol. Chem. , vol.268 , pp. 22004-22009
    • Urade, R.1    Takenaka, Y.2    Kito, M.3
  • 18
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequence of protein disulfide isomerase
    • Mazzarella, R.A., Srinivasan, M., Haugejorden, S.M., and Green, M. (1990) ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequence of protein disulfide isomerase. J. Biol. Chem. 265, 1094-1101
    • (1990) J. Biol. Chem. , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 19
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. and Pelham, H.R.B. (1986) An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291-300
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 20
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. and Pelham, H.R.B. (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 21
    • 0025736560 scopus 로고
    • Analysis of the retention signals of two resident luminal endoplasmic reticulum proteins by in vitro mutagenesis
    • Haugejorden, SM., Srinivasan, M., and Green, M. (1991) Analysis of the retention signals of two resident luminal endoplasmic reticulum proteins by in vitro mutagenesis. J. Biol. Chem. 266, 6015-6018
    • (1991) J. Biol. Chem. , vol.266 , pp. 6015-6018
    • Haugejorden, S.M.1    Srinivasan, M.2    Green, M.3
  • 24
    • 0025914068 scopus 로고
    • A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction
    • Ito, W., Ishiguro, H., and Kurosawa, Y. (1991) A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction. Gene 102, 67-70
    • (1991) Gene , vol.102 , pp. 67-70
    • Ito, W.1    Ishiguro, H.2    Kurosawa, Y.3
  • 25
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C. and Okayama, H. (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7, 2745-2752
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 26
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C.A. and Okayama, H. (1988) Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6, 632-638
    • (1988) BioTechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 29
    • 0028786868 scopus 로고
    • cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum p58: Characterization as a protein disulfide isomerase, but not as a protease or a carnitine acyltransferase
    • Bourdi, M., Demady, D., Martin, J.L., Jabbour, S.K., Martin, B.M., George, J.W., and Pohl, L.R. (1995) cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum p58: Characterization as a protein disulfide isomerase, but not as a protease or a carnitine acyltransferase. Arch. Biochem. Biophys. 323, 397-403
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 397-403
    • Bourdi, M.1    Demady, D.2    Martin, J.L.3    Jabbour, S.K.4    Martin, B.M.5    George, J.W.6    Pohl, L.R.7
  • 30
    • 0030054173 scopus 로고    scopus 로고
    • Cloning, expression and genomic organization of human placental protein disulfide isomerase
    • Charnock-Jones, D., Day, K., and Smith, S.K. (1996) Cloning, expression and genomic organization of human placental protein disulfide isomerase. Int. J. Biochem. Cell Biol. 28, 811-889
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 811-889
    • Charnock-Jones, D.1    Day, K.2    Smith, S.K.3
  • 31
    • 0026700275 scopus 로고
    • Effects of site-directed mutagenesis on the presumed catalytic triad and substrate-binding pocket of grapevine fanleaf nepovirus 24-kDa proteinase
    • Margis, R. and Pinck, L. (1992) Effects of site-directed mutagenesis on the presumed catalytic triad and substrate-binding pocket of grapevine fanleaf nepovirus 24-kDa proteinase. Virology 190, 884-888
    • (1992) Virology , vol.190 , pp. 884-888
    • Margis, R.1    Pinck, L.2
  • 32
    • 0027291014 scopus 로고
    • Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites
    • Kean, K.M., Howell, M.T., Grunert, S., Girard, M., and Jackson, R.L. (1993) Substitution mutations at the putative catalytic triad of the poliovirus 3C protease have differential effects on cleavage at different sites. Virology 194, 360-364
    • (1993) Virology , vol.194 , pp. 360-364
    • Kean, K.M.1    Howell, M.T.2    Grunert, S.3    Girard, M.4    Jackson, R.L.5
  • 33
    • 0027416762 scopus 로고
    • Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: Evidence of a functional relationship with trypsinlike serine proteinase
    • Miyashita, K., Kusumi, M., Utsumi, R., Katayama, S., Noda, M., Komano, T., and Satoh, N. (1993) Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: Evidence of a functional relationship with trypsinlike serine proteinase. Protein Eng. 6, 189-193
    • (1993) Protein Eng. , vol.6 , pp. 189-193
    • Miyashita, K.1    Kusumi, M.2    Utsumi, R.3    Katayama, S.4    Noda, M.5    Komano, T.6    Satoh, N.7


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