메뉴 건너뛰기




Volumn 239, Issue 2, 1996, Pages 509-518

Cyclosporin A inhibits the degradation of signal sequences after processing of presecretory proteins by signal peptidase

Author keywords

Cyclosporin A; Endoplasmic reticulum; Protein degradation; Signal peptidase

Indexed keywords

CYCLOSPORIN A; IMMUNOSUPPRESSIVE AGENT; PUROMYCIN; SIGNAL PEPTIDASE; SIGNAL PEPTIDE;

EID: 0030057070     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0509u.x     Document Type: Article
Times cited : (21)

References (45)
  • 1
    • 0242388325 scopus 로고
    • 1986: A year of new insights into how proteins cross membranes
    • Zimmermann, R. & Meyer, D. I. (1986) 1986: a year of new insights into how proteins cross membranes, Trends Biochem. Sci. 11, 512-515.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 512-515
    • Zimmermann, R.1    Meyer, D.I.2
  • 2
    • 0023689875 scopus 로고
    • Preprotein conformation: The years major theme in translocation studies
    • Meyer, D. I. (1988) Preprotein conformation: the years major theme in translocation studies, Trends Biochem. Sci. 17, 474-478.
    • (1988) Trends Biochem. Sci. , vol.17 , pp. 474-478
    • Meyer, D.I.1
  • 3
    • 0025046014 scopus 로고
    • Protein transport across the ER membrane
    • Rapoport, T. A. (1990) Protein transport across the ER membrane, Trends Biochem. Sci. 15, 355-358.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 355-358
    • Rapoport, T.A.1
  • 4
    • 0026061020 scopus 로고
    • A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation
    • Thrift, R. N., Andrews, D. W., Walter, P. & Johnson, A. E. (1991) A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation, J. Cell Biol. 112, 809-821.
    • (1991) J. Cell Biol. , vol.112 , pp. 809-821
    • Thrift, R.N.1    Andrews, D.W.2    Walter, P.3    Johnson, A.E.4
  • 5
    • 0025858671 scopus 로고
    • The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER
    • High, S., Görlich, D., Wiedmann, M., Rapoport, T. A. & Dobberstein, B. (1991) The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER, J. Cell Biol. 113, 35-44.
    • (1991) J. Cell Biol. , vol.113 , pp. 35-44
    • High, S.1    Görlich, D.2    Wiedmann, M.3    Rapoport, T.A.4    Dobberstein, B.5
  • 6
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich, D., Hartmann, E., Prehn, S. & Rapoport, T. A. (1992) A protein of the endoplasmic reticulum involved early in polypeptide translocation, Nature 357, 47-52.
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapoport, T.A.4
  • 7
    • 0026466143 scopus 로고
    • A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich, D., Prehn, S., Hartmann, E., Kalies, K.-U. & Rapoport, T. A. (1992) A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation, Cell 71, 489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Görlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, K.-U.4    Rapoport, T.A.5
  • 8
    • 0027229977 scopus 로고
    • Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion
    • High, S., Andersen, S. L., Görlich, D., Hartmann, E., Prehn, S., Rapoport, T. A. & Dobberstein, B. (1993) Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion, J. Cell Biol. 121, 743-750.
    • (1993) J. Cell Biol. , vol.121 , pp. 743-750
    • High, S.1    Andersen, S.L.2    Görlich, D.3    Hartmann, E.4    Prehn, S.5    Rapoport, T.A.6    Dobberstein, B.7
  • 9
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum
    • Shaw, A. S., Rottier, P. J. M. & Rose, J. K. (1988) Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum, Proc. Natl Acad. Sci. USA 85, 7592-7596.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 10
    • 0026472576 scopus 로고
    • Structural requirements for transport of preprocecropinA and related precursor proteins into mammalian microsomes
    • Schlenstedt, G., Gudmundsson, G. H., Boman, H. G. & Zimmermann, R. (1992) Structural requirements for transport of preprocecropinA and related precursor proteins into mammalian microsomes, J. Biol. Chem. 267, 24328-24332.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24328-24332
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 11
    • 0019849075 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein
    • Walter, P., Ibrahimi, I. & Blobel, G. (1981) Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein, J. Cell Biol. 91, 545-550.
    • (1981) J. Cell Biol. , vol.91 , pp. 545-550
    • Walter, P.1    Ibrahimi, I.2    Blobel, G.3
  • 12
    • 0023026186 scopus 로고
    • Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein
    • Connolly, T. & Gilmore, R. (1986) Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein, J. Cell Biol. 103, 2253-2261.
    • (1986) J. Cell Biol. , vol.103 , pp. 2253-2261
    • Connolly, T.1    Gilmore, R.2
  • 13
    • 0024400708 scopus 로고
    • Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Römisch, K., Webb, J., Herz, J., Prehn, S., Frank, R., Vingron, M. & Dobberstein, B. (1989) Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains, Nature 340, 478-482.
    • (1989) Nature , vol.340 , pp. 478-482
    • Römisch, K.1    Webb, J.2    Herz, J.3    Prehn, S.4    Frank, R.5    Vingron, M.6    Dobberstein, B.7
  • 14
    • 0024973846 scopus 로고
    • The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide
    • Connolly, T. & Gilmore, R. (1989) The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide, Cell 57, 599-610.
    • (1989) Cell , vol.57 , pp. 599-610
    • Connolly, T.1    Gilmore, R.2
  • 15
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller, J. D., Wilhelm, H., Gierasch, L., Gilmore, R. & Walter, P. (1993) GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation, Nature 366, 351-354.
    • (1993) Nature , vol.366 , pp. 351-354
    • Miller, J.D.1    Wilhelm, H.2    Gierasch, L.3    Gilmore, R.4    Walter, P.5
  • 16
    • 0024507257 scopus 로고
    • Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes
    • Connolly, T., Collins, P. & Gilmore, R. (1989) Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes, J. Cell Biol. 108, 299-307.
    • (1989) J. Cell Biol. , vol.108 , pp. 299-307
    • Connolly, T.1    Collins, P.2    Gilmore, R.3
  • 17
    • 8944236957 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes - A new protease family
    • Dalbey, R. E. & von Heijne, G. (1992) Signal peptidases in prokaryotes and eukaryotes - a new protease family, Trends Biochem. Sci. 18, 334-338.
    • (1992) Trends Biochem. Sci. , vol.18 , pp. 334-338
    • Dalbey, R.E.1    Von Heijne, G.2
  • 18
    • 0025740247 scopus 로고
    • A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes
    • Klappa, P., Mayinger, P., Pipkorn, R., Zimmermann, M. & Zimmermann, R. (1991) A microsomal protein is involved in ATP-dependent transport of presecretory proteins into mammalian microsomes, EMBO J. 10, 2795-2803.
    • (1991) EMBO J. , vol.10 , pp. 2795-2803
    • Klappa, P.1    Mayinger, P.2    Pipkorn, R.3    Zimmermann, M.4    Zimmermann, R.5
  • 19
    • 0025006519 scopus 로고
    • A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and posttranslationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes
    • Schlenstedt, G., Gudmundsson, G. H., Boman, H. G. & Zimmermann, R. (1990) A large presecretory protein translocates both cotranslationally, using signal recognition particle and ribosome, and posttranslationally, without these ribonucleoparticles, when synthesized in the presence of mammalian microsomes, J. Biol. Chem. 265, 13960-13968.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13960-13968
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 20
    • 0028209987 scopus 로고
    • The membrane proteins TRAMp and sec61αp may be involved in posttranslational transport of presecretory proteins into mammalian microsomes
    • Klappa, P., Zimmermann, M. & Zimmermann, R. (1994) The membrane proteins TRAMp and sec61αp may be involved in posttranslational transport of presecretory proteins into mammalian microsomes, FEBS Lett. 341, 281-287.
    • (1994) FEBS Lett. , vol.341 , pp. 281-287
    • Klappa, P.1    Zimmermann, M.2    Zimmermann, R.3
  • 21
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich, D. & Rapoport, T. A. (1993) Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane, Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 22
    • 0014284027 scopus 로고
    • Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex
    • Kobashi, K. (1968) Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex, Biochim. Biophys. Acta 158, 239-245.
    • (1968) Biochim. Biophys. Acta , vol.158 , pp. 239-245
    • Kobashi, K.1
  • 23
    • 0029085091 scopus 로고
    • Protein disulphide isomerase and lumenal cyclophilin-type peptidyl cistrans isomerase are in transient contact with secretory proteins during late stages of translocation
    • Klappa, P., Freedman, R. B. & Zimmermann, R. (1995) Protein disulphide isomerase and lumenal cyclophilin-type peptidyl cistrans isomerase are in transient contact with secretory proteins during late stages of translocation, Eur. J. Biochem. 232, 755-764.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 755-764
    • Klappa, P.1    Freedman, R.B.2    Zimmermann, R.3
  • 24
    • 0027712790 scopus 로고
    • Folding, assembly, and posttranslational modifications of proteins within the lumen of the endoplasmic reticulum
    • Rowling, P. J. E. & Freedman, R. B. (1993) Folding, assembly, and posttranslational modifications of proteins within the lumen of the endoplasmic reticulum, Subcell. Biochem. 21, 41-80.
    • (1993) Subcell. Biochem. , vol.21 , pp. 41-80
    • Rowling, P.J.E.1    Freedman, R.B.2
  • 25
    • 0027748943 scopus 로고
    • Components and mechanisms involved in transport of proteins into the endoplasmic reticulum
    • Klappa, P., Zimmermann, M., Dierks, T. & Zimmermann, R. (1993) Components and mechanisms involved in transport of proteins into the endoplasmic reticulum, Subcell. Biochem. 21, 17-40.
    • (1993) Subcell. Biochem. , vol.21 , pp. 17-40
    • Klappa, P.1    Zimmermann, M.2    Dierks, T.3    Zimmermann, R.4
  • 27
    • 0028500556 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mechanisms of action and cellular physiology
    • Ciechanover, A. (1994) The ubiquitin-mediated proteolytic pathway: mechanisms of action and cellular physiology, Biol. Chem. Hoppe-Seyler 375, 565-581.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 565-581
    • Ciechanover, A.1
  • 28
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters, J.-M. (1994) Proteasomes: protein degradation machines of the cell, Trends Biochem. Sci. 19, 377-382.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377-382
    • Peters, J.-M.1
  • 30
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei, M. L. & Cresswell, P. (1992) HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 356, 443-446.
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 31
    • 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. & 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
  • 32
    • 0027501384 scopus 로고
    • Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum
    • Urade, R., Takenaka, Y. & Kito, M. (1993) Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum, J. Biol. Chem. 268, 22004-22009.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22004-22009
    • Urade, R.1    Takenaka, Y.2    Kito, M.3
  • 33
    • 0021135713 scopus 로고
    • Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity
    • Ichihara, S., Beppu, N. & Mizushima, S. (1984) Protease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity, J. Biol. Chem. 259, 9853-9857.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9853-9857
    • Ichihara, S.1    Beppu, N.2    Mizushima, S.3
  • 34
    • 0026013566 scopus 로고
    • Human cyclophilin B: A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • Price, W. R., Zydowsky, L. D., Jin, M., Baker, C. H., McKeon, F. D. & Walsh, C. T. (1991) Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence, Proc. Natl Acad. Sci. USA 88, 1903-1907.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1903-1907
    • Price, W.R.1    Zydowsky, L.D.2    Jin, M.3    Baker, C.H.4    McKeon, F.D.5    Walsh, C.T.6
  • 35
    • 0027274978 scopus 로고
    • Cyclosporin A, FK506 and rapamycin: More than just immunosuppression
    • Kunz, J. & Hall, M. N. (1993) Cyclosporin A, FK506 and rapamycin: more than just immunosuppression, Trends Biochem. Sci. 18, 334-338.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 334-338
    • Kunz, J.1    Hall, M.N.2
  • 36
    • 0028336648 scopus 로고
    • Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum
    • Bose, S. & Freedman, R. B. (1994) Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum, Biochem. J. 300, 865-870.
    • (1994) Biochem. J. , vol.300 , pp. 865-870
    • Bose, S.1    Freedman, R.B.2
  • 37
    • 0028216390 scopus 로고
    • The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic reticulum
    • Bose, S., Mücke, M. & Freedman, R. B. (1994) The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic reticulum, Biochem. J. 300, 871-875.
    • (1994) Biochem. J. , vol.300 , pp. 871-875
    • Bose, S.1    Mücke, M.2    Freedman, R.B.3
  • 38
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C., Sinskey, A. J. & Lodish, H. F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 39
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra, A. M., Fagioli, C., Finazzi, D., Sitia, R. & Alberini, C. M. (1993) Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation, EMBO J. 12, 4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.M.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.M.5
  • 40
    • 0027721032 scopus 로고
    • The endoplasmic reticulum as a site of protein degradation
    • Fra, A. M. & Sitia, R. (1993) The endoplasmic reticulum as a site of protein degradation, Subcell. Biochem. 21, 143-168.
    • (1993) Subcell. Biochem. , vol.21 , pp. 143-168
    • Fra, A.M.1    Sitia, R.2
  • 41
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans, E. A., Gilmore, R. & Blobel, G. (1986) Purification of microsomal signal peptidase as a complex, Proc. Natl Acad. Sci. USA 83, 581-585.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 42
    • 0023806488 scopus 로고
    • cDNA-derived primary structure of the glycoprotein component of canine microsomal signal peptidase complex
    • Shelness, G. S., Kanwar, Y. S. & Blobel, G. (1988) cDNA-derived primary structure of the glycoprotein component of canine microsomal signal peptidase complex, J. Biol. Chem. 263, 17063-17070.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17063-17070
    • Shelness, G.S.1    Kanwar, Y.S.2    Blobel, G.3
  • 43
    • 0024428204 scopus 로고
    • A subunit of mammalian signal peptidase is homologous to yeast Sec11 protein
    • Greenburg, G., Shelness, G. S. & Blobel, G. (1989) A subunit of mammalian signal peptidase is homologous to yeast Sec11 protein, J. Biol. Chem. 264, 15762-15765.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15762-15765
    • Greenburg, G.1    Shelness, G.S.2    Blobel, G.3
  • 44
    • 0025294104 scopus 로고
    • Two subunits of the canine signal peptidase complex are homologous to yeast Sec11 protein
    • Shelness, G. S. & Blobel, G. (1990) Two subunits of the canine signal peptidase complex are homologous to yeast Sec11 protein, J. Biol. Chem. 265, 9512-9519.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9512-9519
    • Shelness, G.S.1    Blobel, G.2
  • 45
    • 0027958547 scopus 로고
    • Evolutionary conservation of components of the protein translocation complex
    • Hartmann, E., Sommer, T., Prehn, S., Görlich, D., Jentsch, S. & Rapoport, T. A. (1994) Evolutionary conservation of components of the protein translocation complex, Nature 367, 654-657.
    • (1994) Nature , vol.367 , pp. 654-657
    • Hartmann, E.1    Sommer, T.2    Prehn, S.3    Görlich, D.4    Jentsch, S.5    Rapoport, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.