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Volumn 90, Issue 1, 1997, Pages 31-41

Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0031471055     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80311-6     Document Type: Article
Times cited : (213)

References (30)
  • 1
    • 0014770988 scopus 로고
    • Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of polypeptides within ribosomes
    • Blobel, G., and Sabatini, D.D. (1970). Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of polypeptides within ribosomes. J. Cell Biol. 45, 130-145.
    • (1970) J. Cell Biol. , vol.45 , pp. 130-145
    • Blobel, G.1    Sabatini, D.D.2
  • 2
    • 0000999605 scopus 로고
    • Fluorescence lifetime and quenching studies on some interesting diphenylhexatriene membrane probes
    • Cranney, M., Cundall, R.B., Jones, G.R., Richards, J.T., and Thomas, E.W. (1983). Fluorescence lifetime and quenching studies on some interesting diphenylhexatriene membrane probes. Biochim. Biophys. Acta 735, 418-425.
    • (1983) Biochim. Biophys. Acta , vol.735 , pp. 418-425
    • Cranney, M.1    Cundall, R.B.2    Jones, G.R.3    Richards, J.T.4    Thomas, E.W.5
  • 3
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K.S., Reinhart, G.D., and Johnson, A.E. (1993). The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 4
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D., and Johnson, A.E. (1994). Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 5
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., Falcone, D., Lin, J., Andrews, D.W., and Johnson, A.E. (1996). The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85, 369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 6
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A.H., and Blobel, G. (1983). Cell-free translation of messenger RNA in a wheat germ system. Meth. Enzymol. 96, 38-50.
    • (1983) Meth. Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 7
    • 0029033102 scopus 로고
    • Synthesis and secretion of apolipoprotein B from cultured liver cells
    • Ginsberg, H.N. (1995). Synthesis and secretion of apolipoprotein B from cultured liver cells. Curr. Opin. Lipid. 6, 275-280.
    • (1995) Curr. Opin. Lipid. , vol.6 , pp. 275-280
    • Ginsberg, H.N.1
  • 9
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane
    • Hamman, B.D., Chen, J.-C., Johnson, E.E., and Johnson, A.E. (1997). The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane. Cell 89, 535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.-C.2    Johnson, E.E.3    Johnson, A.E.4
  • 11
    • 0029924441 scopus 로고    scopus 로고
    • Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol
    • Hedge, R.S., and Lingappa, V.R. (1996). Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol. Cell 85, 217-228.
    • (1996) Cell , vol.85 , pp. 217-228
    • Hedge, R.S.1    Lingappa, V.R.2
  • 12
  • 13
    • 0018942557 scopus 로고
    • The immunoglobulin n chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments
    • Kehry, M., Ewald, S., Douglas, R., Sibley, C., Raschke, W., Fambrough, D, and Hood, L. (1980). The immunoglobulin n chains of membrane-bound and secreted IgM molecules differ in their C-terminal segments. Cell 21, 393-406.
    • (1980) Cell , vol.21 , pp. 393-406
    • Kehry, M.1    Ewald, S.2    Douglas, R.3    Sibley, C.4    Raschke, W.5    Fambrough, D.6    Hood, L.7
  • 14
    • 0024425706 scopus 로고
    • Protein translocation across the endoplasmic reticulum membrane: Identification by photocrosslinking of a 39 kDa integral membrane glycoprotein as part of a putative translocation tunnel
    • Krieg, U.C., Johnson, A.E., and Walter, P. (1989). Protein translocation across the endoplasmic reticulum membrane: identification by photocrosslinking of a 39 kDa integral membrane glycoprotein as part of a putative translocation tunnel. J. Cell Biol. 109, 2033-2043.
    • (1989) J. Cell Biol. , vol.109 , pp. 2033-2043
    • Krieg, U.C.1    Johnson, A.E.2    Walter, P.3
  • 15
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V., and High, S. (1997). Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem. 272, 1983-1989.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 18
    • 0025239839 scopus 로고
    • Unusual topogenic sequence directs prion protein biogenesis
    • Lopez, C.D., Yost, C.S., Prusiner, S.B., Myers, R.M., and Lingappa, V.R. (1990). Unusual topogenic sequence directs prion protein biogenesis. Science 248, 226-229.
    • (1990) Science , vol.248 , pp. 226-229
    • Lopez, C.D.1    Yost, C.S.2    Prusiner, S.B.3    Myers, R.M.4    Lingappa, V.R.5
  • 19
    • 0014202553 scopus 로고
    • Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding
    • Malkin, L.I., and Rich, A. (1967). Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding. J. Mol. Biol. 26, 329-346.
    • (1967) J. Mol. Biol. , vol.26 , pp. 329-346
    • Malkin, L.I.1    Rich, A.2
  • 20
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M.W., Brunner, J., and Dobberstein, B. (1995). The protein-conducting channel in the membrane of endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 21
    • 0019047935 scopus 로고
    • Biogenesis of membrane-bound and secreted immunoglobulins. I. Two distinct translation products of human μ-chain, with identical N-termini and different C-termini
    • McCune, J.M., Lingappa, V.R., Fu, S.M., Blobel, G., and Kunkel, H.G. (1980). Biogenesis of membrane-bound and secreted immunoglobulins. I. Two distinct translation products of human μ-chain, with identical N-termini and different C-termini. J. Exp. Med. 152, 463-468.
    • (1980) J. Exp. Med. , vol.152 , pp. 463-468
    • McCune, J.M.1    Lingappa, V.R.2    Fu, S.M.3    Blobel, G.4    Kunkel, H.G.5
  • 22
    • 0029952518 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996). Protein translocation across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 23
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 24
    • 0025224551 scopus 로고
    • The structure and insertion of integral proteins in membranes
    • Singer, S.J. (1990). The structure and insertion of integral proteins in membranes. Annu. Rev. Cell Biol. 6, 247-296.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 247-296
    • Singer, S.J.1
  • 25
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach, W.R., and Lingappa, V.R. (1993). Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J. Biol. Chem. 268, 23552-23561.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 26
    • 0024848813 scopus 로고
    • Stop-transfer activity of hydrophobic sequences depends on the translation system
    • Spiess, M., Handschin, C., and Baker, K.P. (1989). Stop-transfer activity of hydrophobic sequences depends on the translation system. J. Biol. Chem. 264, 19117-19124.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19117-19124
    • Spiess, M.1    Handschin, C.2    Baker, K.P.3
  • 27
    • 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., and 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
  • 28
    • 0023816534 scopus 로고
    • Cloning and expression in Escherichia coli of the perfringolysin O(theta-toxin) gene from Clostridium perfringens and characterization of the gene product
    • Tweten, R.K. (1988). Cloning and expression in Escherichia coli of the perfringolysin O(theta-toxin) gene from Clostridium perfringens and characterization of the gene product. Infect. Immun. 56, 3228-3234.
    • (1988) Infect. Immun. , vol.56 , pp. 3228-3234
    • Tweten, R.K.1
  • 29
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and Johnson, A.E. (1994). Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 30
    • 0029112391 scopus 로고
    • NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyltransferase center
    • Wang, S., Sakai, H., and Wiedmann, M. (1995). NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyltransferase center. J. Cell Biol. 130, 519-528.
    • (1995) J. Cell Biol. , vol.130 , pp. 519-528
    • Wang, S.1    Sakai, H.2    Wiedmann, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.