메뉴 건너뛰기




Volumn 10, Issue 5, 1999, Pages 465-472

Role and regulation of the ER chaperone BiP

Author keywords

BiP; Endoplasmic reticulum; HSP70; Molecular chaperone; Protein folding

Indexed keywords

BIOLOGICAL MARKER; FUNGAL PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; KAR2 PROTEIN, YEAST; PEPTIDE;

EID: 0033208953     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0318     Document Type: Article
Times cited : (453)

References (83)
  • 1
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas IG, Wabl M. Immunoglobulin heavy chain binding protein. Nature. 306:1983;387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 2
    • 0017665008 scopus 로고
    • Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation
    • Pouyssegur J, Shiu RPC, Pastan I. Induction of two transformation-sensitive membrane polypeptides in normal fibroblasts by a block in glycoprotein synthesis or glucose deprivation. Cell. 11:1977;941-947.
    • (1977) Cell , vol.11 , pp. 941-947
    • Pouyssegur, J.1    Shiu, R.P.C.2    Pastan, I.3
  • 3
    • 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, Pelham HRB. An Hsp70-like protein in the ER: identity with the 78-kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell. 46:1986;291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 4
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook JF. Protein folding in the cell. Nature. 355:1992;33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.F.2
  • 6
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell. 92:1998;747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 8
    • 0029042422 scopus 로고
    • BiP/Kar2p serves as a molecular chaperone during carboxypepidase Y folding in yeast
    • Simons JF, Ferro-Novick S, Rose MD, Helenius A. BiP/Kar2p serves as a molecular chaperone during carboxypepidase Y folding in yeast. J Cell Biol. 130:1995;41-49.
    • (1995) J Cell Biol , vol.130 , pp. 41-49
    • Simons, J.F.1    Ferro-Novick, S.2    Rose, M.D.3    Helenius, A.4
  • 9
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocation inSaccharomyces cerevisiae
    • Corsi AK, Schekman R. The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocation inSaccharomyces cerevisiae. J Cell Biol. 137:1997;1483-1493.
    • (1997) J Cell Biol , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 10
    • 0031774206 scopus 로고    scopus 로고
    • Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER
    • McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER. Mol Biol Cell. 9:1998;3533-3545.
    • (1998) Mol Biol Cell , vol.9 , pp. 3533-3545
    • McClellan, A.J.1    Endres, J.B.2    Vogel, J.P.3    Palazzi, D.4    Rose, M.D.5    Brodsky, J.L.6
  • 11
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky JL, Werner ED, Dubas ME, Goeckeler JL, Kruse KB, McCracken AA. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J Biol Chem. 274:1999;3453-3460.
    • (1999) J Biol Chem , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 12
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper RK, Bohmler S, Bordallo J, Sommer T, Wolf DH. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:1997;891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 13
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homologue of mammalian BiP/GRP78
    • Rose MD, Misra LM, Vogel JP. KAR2, a karyogamy gene, is the yeast homologue of mammalian BiP/GRP78. Cell. 57:1989;1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 14
    • 0028365624 scopus 로고
    • The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion
    • Latterich M, Schekman R. The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. Cell. 78:1994;87-98.
    • (1994) Cell , vol.78 , pp. 87-98
    • Latterich, M.1    Schekman, R.2
  • 15
    • 0030051440 scopus 로고    scopus 로고
    • ER membrane protein complex required for nuclear fusion
    • Ng DTW, Walter P. ER membrane protein complex required for nuclear fusion. J Cell Biol. 132:1996;499-509.
    • (1996) J Cell Biol , vol.132 , pp. 499-509
    • Ng, D.T.W.1    Walter, P.2
  • 16
    • 0027818242 scopus 로고
    • Structure and mechanism of 70-kDa heat-shock-related proteins
    • McKay DB. Structure and mechanism of 70-kDa heat-shock-related proteins. Adv Prot Chem. 44:1993;67-80.
    • (1993) Adv Prot Chem , vol.44 , pp. 67-80
    • McKay, D.B.1
  • 17
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn GC, Chappell TG, Rothman JE. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science. 245:1989;385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 19
    • 0027164203 scopus 로고
    • Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
    • Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJH. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers. J Biol Chem. 268:1993;12730-12735.
    • (1993) J Biol Chem , vol.268 , pp. 12730-12735
    • Blond-Elguindi, S.1    Fourie, A.M.2    Sambrook, J.F.3    Gething, M.J.H.4
  • 20
    • 0028149893 scopus 로고
    • Common and divergent peptide binding specificities of hsp70 molecular chaperones
    • Fourie AM, Sambrook JF, Gething MJH. Common and divergent peptide binding specificities of hsp70 molecular chaperones. J Biol Chem. 269:1994;30470-30478.
    • (1994) J Biol Chem , vol.269 , pp. 30470-30478
    • Fourie, A.M.1    Sambrook, J.F.2    Gething, M.J.H.3
  • 22
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70-K heat-shock cognate protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB. Three-dimensional structure of the ATPase fragment of a 70-K heat-shock cognate protein. Nature. 346:1990;623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 24
    • 0032500673 scopus 로고    scopus 로고
    • Substrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP
    • Chevalier M, King L, Wang C, Gething MJ, Elguindi E, Blond SY. Substrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP. J Biol Chem. 273:1998;26827-26835.
    • (1998) J Biol Chem , vol.273 , pp. 26827-26835
    • Chevalier, M.1    King, L.2    Wang, C.3    Gething, M.J.4    Elguindi, E.5    Blond, S.Y.6
  • 26
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association of BiP with newly synthsized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • Hellman R, Vanhove M, Lejeune A, Stevens FJ, Mendershot LM. The in vivo association of BiP with newly synthsized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. Cell Biol. 144:1999;21-30.
    • (1999) Cell Biol , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhove, M.2    Lejeune, A.3    Stevens, F.J.4    Mendershot, L.M.5
  • 27
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr DM, Langer L, Douglas MG. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. TIBS. 19:1994;176-181.
    • (1994) TIBS , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, L.2    Douglas, M.G.3
  • 28
    • 0026690820 scopus 로고
    • Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
    • Feldheim D, Rothblatt J, Schekman R. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol Cell Biol. 12:1992;3288-3296.
    • (1992) Mol Cell Biol , vol.12 , pp. 3288-3296
    • Feldheim, D.1    Rothblatt, J.2    Schekman, R.3
  • 29
    • 0029021905 scopus 로고
    • A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
    • Schlenstedt G, Harris S, Risse B, Lill R, Silver PA. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol. 129:1995;979-988.
    • (1995) J Cell Biol , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.A.5
  • 30
    • 0030949349 scopus 로고    scopus 로고
    • The yeast Jem1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
    • Nishikawa S, Endo T. The yeast Jem1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion. J Biol Chem. 272:1997;12889-12892.
    • (1997) J Biol Chem , vol.272 , pp. 12889-12892
    • Nishikawa, S.1    Endo, T.2
  • 31
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky JL, Schekman R. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol. 123:1993;1355-1363.
    • (1993) J Cell Biol , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 32
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman SK, Schekman R. Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell. 88:1997;85-96.
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 33
    • 0032214832 scopus 로고    scopus 로고
    • J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
    • Misselwitz B, Staeck O, Rapoport TA. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell. 2:1998;593-603.
    • (1998) Mol Cell , vol.2 , pp. 593-603
    • Misselwitz, B.1    Staeck, O.2    Rapoport, T.A.3
  • 34
    • 0028893336 scopus 로고
    • Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins
    • Brightman SE, Blatch GL, Zetter BR. Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins. Gene. 153:1995;249-254.
    • (1995) Gene , vol.153 , pp. 249-254
    • Brightman, S.E.1    Blatch, G.L.2    Zetter, B.R.3
  • 35
    • 0032539016 scopus 로고    scopus 로고
    • A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum
    • Silberstein S, Schlenstedt G, Silver PA, Gilmore R. A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum. J Cell Biol. 143:1998;921-933.
    • (1998) J Cell Biol , vol.143 , pp. 921-933
    • Silberstein, S.1    Schlenstedt, G.2    Silver, P.A.3    Gilmore, R.4
  • 36
    • 0023684672 scopus 로고
    • Identity of the immunoglobulin heavychain-binding protein with the 78"000-dalton glucose-regulated protein and the role of post-translational modifications in its binding function
    • Hendershot LM, Ting J, Lee AS. Identity of the immunoglobulin heavychain-binding protein with the 78"000-dalton glucose-regulated protein and the role of post-translational modifications in its binding function. Mol Cell Biol. 8:1988;4250-4256.
    • (1988) Mol Cell Biol , vol.8 , pp. 4250-4256
    • Hendershot, L.M.1    Ting, J.2    Lee, A.S.3
  • 37
    • 0026567520 scopus 로고
    • Interconversion of three differently modified and assembled forms of BiP
    • Freiden PJ, Gaut JR, Hendershot LM. Interconversion of three differently modified and assembled forms of BiP. EMBO J. 11:1992;63-70.
    • (1992) EMBO J , vol.11 , pp. 63-70
    • Freiden, P.J.1    Gaut, J.R.2    Hendershot, L.M.3
  • 38
    • 0026523153 scopus 로고
    • Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: Multiple species and disaggregation
    • Carlino A, Toledo H, Skaleris D, DeLisio R, Weissbach H, Brot N. Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation. Proc Natl Acad Sci. 89:1992;2081-2085.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 2081-2085
    • Carlino, A.1    Toledo, H.2    Skaleris, D.3    Delisio, R.4    Weissbach, H.5    Brot, N.6
  • 40
    • 0026051442 scopus 로고
    • Calcium-dependent autophosphorylation of the glucose-regulated protein, grp78
    • Leustek T, Toledo H, Brot N, Weissbach H. Calcium-dependent autophosphorylation of the glucose-regulated protein, grp78. Arch Biochem Biophys. 289:1991;256-261.
    • (1991) Arch Biochem Biophys , vol.289 , pp. 256-261
    • Leustek, T.1    Toledo, H.2    Brot, N.3    Weissbach, H.4
  • 41
    • 0031474105 scopus 로고    scopus 로고
    • In vivo threonine phosphorylation of immunoglobulin binding protein (BiP) maps to its protein binding domain
    • Gaut JR. In vivo threonine phosphorylation of immunoglobulin binding protein (BiP) maps to its protein binding domain. Cell Stress Chaperones. 2:1997;252-262.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 252-262
    • Gaut, J.R.1
  • 42
    • 0020807492 scopus 로고
    • r83"000 stress-inducible and glucose-regulated protein in avian and mammalian cells: Modulation by heat shock and glucose starvation
    • r83"000 stress-inducible and glucose-regulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation. Proc Natl Acad Sci USA. 80:1983;4664-4668.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4664-4668
    • Carlsson, L.1    Lazarides, E.2
  • 43
    • 0025674402 scopus 로고
    • Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein
    • Leno GH, Ledford BE. Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein. FEBS. 276:1990;29-33.
    • (1990) FEBS , vol.276 , pp. 29-33
    • Leno, G.H.1    Ledford, B.E.2
  • 44
    • 0028134743 scopus 로고
    • ADP-ribosylation of the molecular chaperone GRP78/BiP
    • Ledford BE, Leno GH. ADP-ribosylation of the molecular chaperone GRP78/BiP. Mol Cell Biochem. 138:1994;141-148.
    • (1994) Mol Cell Biochem , vol.138 , pp. 141-148
    • Ledford, B.E.1    Leno, G.H.2
  • 45
    • 0032897211 scopus 로고    scopus 로고
    • The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing
    • Laitusis AL, Brostrom MA, Brostrom CO. The dynamic role of GRP78/BiP in the coordination of mRNA translation with protein processing. J Biol Chem. 274:1999;486-493.
    • (1999) J Biol Chem , vol.274 , pp. 486-493
    • Laitusis, A.L.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 46
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick J, Dul JL, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature. 370:1994;373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 47
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C, Helenius A. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science. 266:1994;456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 48
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular cha perones during thyroglobulin folding in the endoplasmic reticulum
    • Kim PS, Arvan P. Calnexin and BiP act as sequential molecular cha perones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol. 128:1995;29-38.
    • (1995) J Cell Biol , vol.128 , pp. 29-38
    • Kim, P.S.1    Arvan, P.2
  • 49
    • 0027136174 scopus 로고
    • The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
    • Lin H, Masso-Welch P, Di Y-P, Cai J, Shen J, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol Biol Cell. 4:1993;1109-1119.
    • (1993) Mol Biol Cell , vol.4 , pp. 1109-1119
    • Lin, H.1    Masso-Welch, P.2    Di Y-P3    Cai, J.4    Shen, J.5    Subjeck, J.R.6
  • 50
    • 14444280363 scopus 로고    scopus 로고
    • Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum
    • Kuznetsov G, Chen LB, Nigam SK. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem. 272:1997;3057-3063.
    • (1997) J Biol Chem , vol.272 , pp. 3057-3063
    • Kuznetsov, G.1    Chen, L.B.2    Nigam, S.K.3
  • 51
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu U, Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol. 136:1997;555-565.
    • (1997) J Cell Biol , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 52
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose JK, Doms RW. Regulation of protein export from the endoplasmic reticulum. Ann Rev Cell Biol. 4:1988;257-288.
    • (1988) Ann Rev Cell Biol , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 53
    • 0028077034 scopus 로고
    • The cellular response to unfolded proteins: Intercompartmental signaling
    • McMillan DR, Gething MJ, Sambrook J. The cellular response to unfolded proteins: intercompartmental signaling. Curr Biol. 5:1994;540-545.
    • (1994) Curr Biol , vol.5 , pp. 540-545
    • McMillan, D.R.1    Gething, M.J.2    Sambrook, J.3
  • 54
    • 0028084733 scopus 로고
    • The unfolded-protein-response pathway in yeast
    • Shamu CE, Cox JS, Walter P. The unfolded-protein-response pathway in yeast. Trends Cell Biol. 4:1994;56-60.
    • (1994) Trends Cell Biol , vol.4 , pp. 56-60
    • Shamu, C.E.1    Cox, J.S.2    Walter, P.3
  • 55
    • 35848968250 scopus 로고    scopus 로고
    • Signalling of the unfolded protein response from the endoplasmic reticulum to the nucleus
    • Gething M. J, Oxford: Oxford University Press
    • McNees C, Gething M-J. Signalling of the unfolded protein response from the endoplasmic reticulum to the nucleus, Gething M J,. Guidebook to Molecular Chaperones and Protein-Folding Catalysts. 1997;541-549 Oxford University Press, Oxford.
    • (1997) Guidebook to Molecular Chaperones and Protein-Folding Catalysts , pp. 541-549
    • McNees, C.1    Gething M-J2
  • 56
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno K, Normington K, Sambrook J, Gething M-J, Mori K. The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol. 13:1993;877-890.
    • (1993) Mol Cell Biol , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething M-J4    Mori, K.5
  • 57
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose regulated proteins. Nature. 332:1988;462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 58
    • 0026628290 scopus 로고
    • A 22-bp cis -acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, Sant A, Kohno K, Normington K, Gething M-J, Sambrook JF. A 22-bp cis -acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11:1992;2583-2593.
    • (1992) EMBO J , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething M-J5    Sambrook, J.F.6
  • 59
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington K, Kohno K, Kozutsumi Y, Gething MJ, Sambrook J. S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell. 57:1989;1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 60
    • 0032540253 scopus 로고    scopus 로고
    • Palindrome with s pacer of one nucleotide is characteristic of the cis -acting unfolded protein response element in Saccharomyces cerevisiae
    • Mori K, Ogawa N, Kawahara T, Yanagi H, Yura T. Palindrome with s pacer of one nucleotide is characteristic of the cis -acting unfolded protein response element in Saccharomyces cerevisiae. J Biol Chem. 730:1998;9912-9920.
    • (1998) J Biol Chem , vol.730 , pp. 9912-9920
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, H.4    Yura, T.5
  • 61
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis -acting endoplasmic reticulum stress response element responsible for the transcriptional induction of mammalian glucose-regulated proteins
    • Yoshida H, Haze K, Yanagi H, Yura T, Mori K. Identification of the cis -acting endoplasmic reticulum stress response element responsible for the transcriptional induction of mammalian glucose-regulated proteins. J Biol Chem. 273:1998;33741-33749.
    • (1998) J Biol Chem , vol.273 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 62
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori K, Ma W, Gething M-J, Sambrook J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell. 74:1993;743-756.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething M-J3    Sambrook, J.4
  • 63
    • 0030228708 scopus 로고    scopus 로고
    • Signaling from the ER to the nucleus: Transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway
    • Mori K, Kawahara T, Yoshida H, Yanagi H, Yura T. Signaling from the ER to the nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway. Genes Cells. 1:1996;803-817.
    • (1996) Genes Cells , vol.1 , pp. 803-817
    • Mori, K.1    Kawahara, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5
  • 64
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell. 73:1993;1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 65
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox JS, Walter P. A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell. 87:1996;391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 66
    • 0030297538 scopus 로고    scopus 로고
    • TRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • Sidrauski C, Cox JS, Walter P. tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell. 87:1996;405-413.
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 67
    • 0003157792 scopus 로고
    • Modular units of heat shock regulatory regions: Structure and function in stress proteins
    • R. I, Morimoto, A, Tissiéres, Georgopoulos C, New York: Cold Spring Harbor Press
    • Lis JT, Xiao H, Perisic O. Modular units of heat shock regulatory regions: structure and function in stress proteins, Morimoto R I, Tissiéres A, Georgopoulos C,. Biology and Medicine. 1990;411-428 Cold Spring Harbor Press, New York.
    • (1990) Biology and Medicine , pp. 411-428
    • Lis, J.T.1    Xiao, H.2    Perisic, O.3
  • 68
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • Shamu CE, Walter P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15:1996;3028-3039.
    • (1996) EMBO J , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 69
    • 0029892851 scopus 로고    scopus 로고
    • The unfolded protein response pathway in Saccharomyces cerevisiae
    • Welihinda AA, Kaufman RJ. The unfolded protein response pathway in Saccharomyces cerevisiae. J Biol Chem. 271:1996;18181-18187.
    • (1996) J Biol Chem , vol.271 , pp. 18181-18187
    • Welihinda, A.A.1    Kaufman, R.J.2
  • 70
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • Sidrauski C, Walter P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell. 90:1997;1-20.
    • (1997) Cell , vol.90 , pp. 1-20
    • Sidrauski, C.1    Walter, P.2
  • 71
    • 0030945046 scopus 로고    scopus 로고
    • Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p
    • Welihinda AA, Tirasophon W, Green SR, Kaufman RJ. Gene induction in response to unfolded protein in the endoplasmic reticulum is mediated through Ire1p kinase interaction with a transcriptional coactivator complex containing Ada5p. Proc Natl Acad Sci USA. 94:1997;4289-4294.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4289-4294
    • Welihinda, A.A.1    Tirasophon, W.2    Green, S.R.3    Kaufman, R.J.4
  • 72
    • 0031948846 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase Ptc2p negative regulates the unfolded-protein repsonse by dephosphorylating Ire1p kinase
    • Welihinda AA, Tirasophon W, Green SR, Kaufnian RJ. Protein serine/threonine phosphatase Ptc2p negative regulates the unfolded-protein repsonse by dephosphorylating Ire1p kinase. Mol Cell Biol. 18:1998;1967-1977.
    • (1998) Mol Cell Biol , vol.18 , pp. 1967-1977
    • Welihinda, A.A.1    Tirasophon, W.2    Green, S.R.3    Kaufnian, R.J.4
  • 73
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon W, Welihinda AA, Kauftnan RJ. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12:1998;1812-1824.
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kauftnan, R.J.3
  • 74
    • 0032190546 scopus 로고    scopus 로고
    • Cloning of mammalian Ire1 reveals diversity in the ER stress responses
    • Wang X-Z, Harding HP, Zhang Y, Jolicoleu EM, Kuroda M, Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J. 17:1998;5708-5717.
    • (1998) EMBO J , vol.17 , pp. 5708-5717
    • Wang X-Z1    Harding, H.P.2    Zhang, Y.3    Jolicoleu, E.M.4    Kuroda, M.5    Ron, D.6
  • 75
    • 0031941355 scopus 로고    scopus 로고
    • Unconventional splicing of HAC1/ERN4 mRNA required for the unfolded protein response. Sequence-specific and non-sequential cleavage of the specific sites
    • Kawahara T, Yanagi H, Yura T, Mori K. Unconventional splicing of HAC1/ERN4 mRNA required for the unfolded protein response. Sequence-specific and non-sequential cleavage of the specific sites. J Biol Chem. 273:1998;1802-1807.
    • (1998) J Biol Chem , vol.273 , pp. 1802-1807
    • Kawahara, T.1    Yanagi, H.2    Yura, T.3    Mori, K.4
  • 76
    • 0027729197 scopus 로고
    • Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticulum stress
    • Prostko CR, Brostrom MA, Brostrom CO. Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticulum stress. Mol Cell Biochem. 1993;127-128:
    • (1993) Mol Cell Biochem , pp. 127-128
    • Prostko, C.R.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 77
    • 0031961688 scopus 로고    scopus 로고
    • Regulation of translational initiation during the cellular response to stress
    • Brostrom CO, Brostrom MA. Regulation of translational initiation during the cellular response to stress. Prog Nucleic Acid Res Mol Biol. 58:1998;79-125.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.58 , pp. 79-125
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 78
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum resident kinase
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum resident kinase. Nature. 397:1999;271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 79
    • 0026468393 scopus 로고
    • Establishment of a chinese hamster ovary cell line that expresses grp78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94
    • Li L-J, Li V, Ferrario A, Rucker N, Liu ES, Wong S, Gomer CJ, Lee AS. Establishment of a chinese hamster ovary cell line that expresses grp78 antisense transcripts and suppresses A23187 induction of both GRP78 and GRP94. J Cell Physiol. 153:1992;575-582.
    • (1992) J Cell Physiol , vol.153 , pp. 575-582
    • Li L-J1    Li, V.2    Ferrario, A.3    Rucker, N.4    Liu, E.S.5    Wong, S.6    Gomer, C.J.7    Lee, A.S.8
  • 80
    • 0028927489 scopus 로고
    • Generation of a mammalian cell line deficient in glucose-regulated protein stress induction through targeted ribozyme driven by a stress-inducible promoter
    • Little E, Lee AS. Generation of a mammalian cell line deficient in glucose-regulated protein stress induction through targeted ribozyme driven by a stress-inducible promoter. J Biol Chem. 27:1995;9526-9534.
    • (1995) J Biol Chem , vol.27 , pp. 9526-9534
    • Little, E.1    Lee, A.S.2
  • 81
    • 0032230314 scopus 로고    scopus 로고
    • Enhanced binding to the molecular chaperone B iP slows thyroglobulin export from the endoplasmic reticulum
    • Muresan Z, Arvan P. Enhanced binding to the molecular chaperone B iP 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
  • 82
    • 0027182875 scopus 로고
    • BiP binds type I procollagen pro-alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler SD, Byers PH. BiP binds type I procollagen pro-alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J Biol Chem. 268:1993;18226-18233.
    • (1993) J Biol Chem , vol.268 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 83
    • 0032918044 scopus 로고    scopus 로고
    • A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse
    • Wang J, Takeuchi T, Tanaka S, Kubo SK, Kayo T, Lu D, Takata K, Koizumi A, Izumi T. A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. J Clin Invest. 103:1999;27-37.
    • (1999) J Clin Invest , vol.103 , pp. 27-37
    • Wang, J.1    Takeuchi, T.2    Tanaka, S.3    Kubo, S.K.4    Kayo, T.5    Lu, D.6    Takata, K.7    Koizumi, A.8    Izumi, T.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.