메뉴 건너뛰기




Volumn 354, Issue 1, 2007, Pages 315-320

The binding of FKBP23 to BiP modulates BiP's ATPase activity with its PPIase activity

Author keywords

ATPase activity; BiP; Ca2+ binding relationship; FK506 binding protein; PPIase activity

Indexed keywords

ADENOSINE TRIPHOSPHATASE; FK 506 BINDING PROTEIN; FK 506 BINDING PROTEIN 23; GLUCOSE REGULATED PROTEIN 78; PEPTIDYLPROLYL ISOMERASE; UNCLASSIFIED DRUG;

EID: 33846444710     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.209     Document Type: Article
Times cited : (16)

References (31)
  • 1
    • 0026625939 scopus 로고
    • Immunophilin-sensitive protein phosphatase action in cell signaling pathways
    • Schreiber S.L. Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell 70 (1992) 365-368
    • (1992) Cell , vol.70 , pp. 365-368
    • Schreiber, S.L.1
  • 2
    • 0028050923 scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and their effectors
    • Fischer G. Peptidyl-prolyl cis/trans isomerases and their effectors. Angew. Chem. 33 (1994) 1415-1436
    • (1994) Angew. Chem. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 5
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas I.G., and 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
  • 6
    • 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. 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.2
  • 7
    • 0024121547 scopus 로고
    • cDNA cloning of the immunoglobulin heavy chain binding protein
    • Haas I.G., and Meo T. cDNA cloning of the immunoglobulin heavy chain binding protein. Proc. Natl. Acad. Sci. USA 85 (1988) 2250-2254
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2250-2254
    • Haas, I.G.1    Meo, T.2
  • 8
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper R.K., Bohmler S., Bordallo J., Sommer T., and Wolf D.H. 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
  • 9
    • 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 J.L., Werner E.D., Dubas M.E., Goeckeler J.L., Kruse K.B., and McCracken A.A. 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
  • 10
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa S.I., Fewell S.W., Kato Y., Brodsky J.L., and Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153 (2001) 1061-1070
    • (2001) J. Cell Biol. , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 11
    • 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 B.D., Hendershot L.M., and Johnson A.E. 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
  • 13
    • 0035955614 scopus 로고    scopus 로고
    • Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates
    • Stronge V.S., Saito Y., Ihara Y., and Williams D.B. Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates. J. Biol. Chem. 276 (2001) 39779-39787
    • (2001) J. Biol. Chem. , vol.276 , pp. 39779-39787
    • Stronge, V.S.1    Saito, Y.2    Ihara, Y.3    Williams, D.B.4
  • 14
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh N.G., and Johnson A.E. A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membrane. J. Cell Biol. 156 (2002) 261-270
    • (2002) J. Cell Biol. , vol.156 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 16
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rudiger S., Buchberger A., and Bukau B. Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4 (1997) 342-349
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 342-349
    • Rudiger, S.1    Buchberger, A.2    Bukau, B.3
  • 17
    • 0034397884 scopus 로고    scopus 로고
    • Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch
    • Rudiger S., Mayer M.P., Schneider-Mergener J., and Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J. Mol. Biol. 304 (2000) 245-251
    • (2000) J. Mol. Biol. , vol.304 , pp. 245-251
    • Rudiger, S.1    Mayer, M.P.2    Schneider-Mergener, J.3    Bukau, B.4
  • 18
    • 0024325535 scopus 로고
    • Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
    • Kassenbrock C.K., and Kelly R.B. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J. 8 (1989) 1461-1467
    • (1989) EMBO J. , vol.8 , pp. 1461-1467
    • Kassenbrock, C.K.1    Kelly, R.B.2
  • 19
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human Hsp90 by a client protein
    • Mclaughlin S.H., Smith H.W., and Jackson S.E. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J. Mol. Biol. 315 (2002) 787-798
    • (2002) J. Mol. Biol. , vol.315 , pp. 787-798
    • Mclaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 20
    • 0033594405 scopus 로고    scopus 로고
    • Molecular chaperones: How J domains turn on Hsp70s
    • Kelley W.L. Molecular chaperones: How J domains turn on Hsp70s. Curr. Biol. 9 (1999) 305-308
    • (1999) Curr. Biol. , vol.9 , pp. 305-308
    • Kelley, W.L.1
  • 22
    • 0037666981 scopus 로고    scopus 로고
    • Modulation of the ATPase cycle of BiP by peptides and proteins
    • Mayer M., Reinstein J., and Buchner J. Modulation of the ATPase cycle of BiP by peptides and proteins. J. Mol. Biol. 330 (2003) 137-144
    • (2003) J. Mol. Biol. , vol.330 , pp. 137-144
    • Mayer, M.1    Reinstein, J.2    Buchner, J.3
  • 23
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., and Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67 (1988) 31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 24
    • 0020528417 scopus 로고
    • Isolation and characterization of the Neurospora crassa endoplasmic reticulum
    • Borgeson C.E., and Bowman B.J. Isolation and characterization of the Neurospora crassa endoplasmic reticulum. J. Bacteriol. 156 (1983) 362-368
    • (1983) J. Bacteriol. , vol.156 , pp. 362-368
    • Borgeson, C.E.1    Bowman, B.J.2
  • 25
    • 0022454127 scopus 로고
    • Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA
    • Morrical S.W., Lee J., and Cox M.M. Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry 25 (1986) 1482-1494
    • (1986) Biochemistry , vol.25 , pp. 1482-1494
    • Morrical, S.W.1    Lee, J.2    Cox, M.M.3
  • 26
    • 0029154926 scopus 로고
    • RuvB protein-mediated ATP hydrolysis: functional asymmetry in the RuvB hexamer
    • Marrione P.E., and Cox M.M. RuvB protein-mediated ATP hydrolysis: functional asymmetry in the RuvB hexamer. Biochemistry 34 (1995) 9809-9818
    • (1995) Biochemistry , vol.34 , pp. 9809-9818
    • Marrione, P.E.1    Cox, M.M.2
  • 27
    • 0026012156 scopus 로고
    • FK506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae
    • Heitman J., Movva N.R., Hiestand P.C., and Hall M.N. FK506-binding protein proline rotamase is a target for the immunosuppressive agent FK506 in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88 (1991) 1948-1952
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1948-1952
    • Heitman, J.1    Movva, N.R.2    Hiestand, P.C.3    Hall, M.N.4
  • 28
    • 0024454546 scopus 로고
    • Perturbation of cellula calcium induces secretion of luminal ER proteins
    • Booth C., and Koch G.L. Perturbation of cellula calcium induces secretion of luminal ER proteins. Cell 59 (1989) 729-737
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 29
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish H.F., and Kong N. Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J. Biol. Chem. 265 (1990) 10893-10899
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 30
    • 0027210895 scopus 로고
    • Unfolded H2b asialoglyco-protein receptor subunit polypeptides are selectively degraded within the endoplasmic reticulum
    • Wikstrom L., and Lodish H.F. Unfolded H2b asialoglyco-protein receptor subunit polypeptides are selectively degraded within the endoplasmic reticulum. J. Biol. Chem. 268 (1993) 14412-14416
    • (1993) J. Biol. Chem. , vol.268 , pp. 14412-14416
    • Wikstrom, L.1    Lodish, H.F.2
  • 31
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan T., Rizzuto R., Volpe P., and Meldolesi J. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74 (1994) 595-636
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.