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Volumn 5, Issue 2, 2013, Pages

Protein translocation across the rough endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; MEMBRANE PROTEIN; MESSENGER RNA; SIGNAL PEPTIDE;

EID: 84870760195     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a013342     Document Type: Article
Times cited : (56)

References (154)
  • 1
    • 0028125253 scopus 로고
    • The SRP54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe
    • Althoff SM, Stevens SW, Wise JA. 1994. The SRP54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe. Mol Cell Biol 14: 7839-7854.
    • (1994) Mol Cell Biol , vol.14 , pp. 7839-7854
    • Althoff, S.M.1    Stevens, S.W.2    Wise, J.A.3
  • 2
    • 0023443260 scopus 로고
    • Evidence for an extended 7SL RNA structure in the signal recognition particle
    • Andrews D, Walter P, Ottensmeyer FP. 1987. Evidence for an extended 7SL RNA structure in the signal recognition particle. EMBO J 6: 3471-3477.
    • (1987) EMBO J , vol.6 , pp. 3471-3477
    • Andrews, D.1    Walter, P.2    Ottensmeyer, F.P.3
  • 3
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA. 2000. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 287: 1232-1239.
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 7
    • 60849096653 scopus 로고    scopus 로고
    • A signal-anchor sequence stimulates signal recognition particle bindingto ribosomes from inside the exit tunnel
    • Berndt U, Oellerer S, Zhang Y, Johnson AE, Rospert S. 2009. A signal-anchor sequence stimulates signal recognition particle bindingto ribosomes from inside the exit tunnel. Proc Natl Acad Sci 106: 1398-1403.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 1398-1403
    • Berndt, U.1    Oellerer, S.2    Zhang, Y.3    Johnson, A.E.4    Rospert, S.5
  • 8
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S, Walter P. 1989. Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340: 482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 9
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytic processed and unprocessed nascent immunoglobulin light chains on membrane bound ribosomes of murine myeloma
    • Blobel G, Dobberstein B. 1975. Transfer of proteins across membranes. I. Presence of proteolytic processed and unprocessed nascent immunoglobulin light chains on membrane bound ribosomes of murine myeloma. J Cell Biol 67: 835-851.
    • (1975) J Cell Biol , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 10
    • 79851511792 scopus 로고    scopus 로고
    • Targeting pathways of C-tailanchored proteins
    • Borgese N, Fasana E. 2011. Targeting pathways of C-tailanchored proteins. Biochim Biophys Acta 1808: 937-946.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 937-946
    • Borgese, N.1    Fasana, E.2
  • 11
    • 43249083239 scopus 로고    scopus 로고
    • Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
    • Bornemann T, Jockel J, Rodnina MV, Wintermeyer W. 2008. Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel. Nat Struct Mol Biol 15: 494-499.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 494-499
    • Bornemann, T.1    Jockel, J.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 12
    • 0023991351 scopus 로고
    • Identification of an essential Schizosaccharomyces pombe RNA homologousto the 7SL component of signal recognition particle
    • Brennwald P, Liao X, Holm K, Porter G, Wise JA. 1988. Identification of an essential Schizosaccharomyces pombe RNA homologousto the 7SL component of signal recognition particle. Mol Cell Biol 8: 1580-1590.
    • (1988) Mol Cell Biol , vol.8 , pp. 1580-1590
    • Brennwald, P.1    Liao, X.2    Holm, K.3    Porter, G.4    Wise, J.A.5
  • 13
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both coand posttranslational protein translocation into the yeast endoplasmic reticulum
    • Brodsky JL, Goeckeler J, Schekman R. 1995. BiP and Sec63p are required for both coand posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci 92: 9643-9646.
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckeler, J.2    Schekman, R.3
  • 14
    • 18544380083 scopus 로고    scopus 로고
    • Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
    • Cannon KS, Or E, Clemons WM Jr, Shibata Y, Rapoport TA. 2005. Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. J Cell Biol 169: 219-225.
    • (2005) J Cell Biol , vol.169 , pp. 219-225
    • Cannon, K.S.1    Or, E.2    Clemons Jr., W.M.3    Shibata, Y.4    Rapoport, T.A.5
  • 15
    • 79960316086 scopus 로고    scopus 로고
    • Hierarchical regulation of mRNA partitioning between the cytoplasm and the endoplasmic reticulum of mammalian cells
    • Chen Q, Jagannathan S, Reid DW, Zheng T, Nicchitta CV. 2011. Hierarchical regulation of mRNA partitioning between the cytoplasm and the endoplasmic reticulum of mammalian cells. Mol Biol Cell 22: 2646-2658.
    • (2011) Mol Biol Cell , vol.22 , pp. 2646-2658
    • Chen, Q.1    Jagannathan, S.2    Reid, D.W.3    Zheng, T.4    Nicchitta, C.V.5
  • 16
    • 33749518904 scopus 로고    scopus 로고
    • Slow translocon gating causes cytosolic exposure of transmembrane and lumenal domains during membrane protein integration
    • Cheng Z, Gilmore R. 2006. Slow translocon gating causes cytosolic exposure of transmembrane and lumenal domains during membrane protein integration. Nat Struct Mol Biol 13: 930-936.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 930-936
    • Cheng, Z.1    Gilmore, R.2
  • 17
    • 12144272096 scopus 로고    scopus 로고
    • Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation
    • Cheng Z, Jiang Y, Mandon EC, Gilmore R. 2005. Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J Cell Biol 168: 67-77.
    • (2005) J Cell Biol , vol.168 , pp. 67-77
    • Cheng, Z.1    Jiang, Y.2    Mandon, E.C.3    Gilmore, R.4
  • 18
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico WJ, Waters MG, Blobel G. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 322: 805-810.
    • (1988) Nature , vol.322 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 19
    • 0033153107 scopus 로고    scopus 로고
    • Shape of large bound polysomes in cultured fibroblasts and thyroid epithelial cells
    • Christensen AK, Bourne CM. 1999. Shape of large bound polysomes in cultured fibroblasts and thyroid epithelial cells. Anat Rec 255: 116-129.
    • (1999) Anat Rec , vol.255 , pp. 116-129
    • Christensen, A.K.1    Bourne, C.M.2
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0027361668 scopus 로고
    • GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor
    • Connolly T, Gilmore R. 1993. GTP hydrolysis by complexes of the signal recognition particle and the signal recognition particle receptor. J Cell Biol 123: 799-807.
    • (1993) J Cell Biol , vol.123 , pp. 799-807
    • Connolly, T.1    Gilmore, R.2
  • 23
    • 0026326816 scopus 로고
    • Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor
    • Connolly T, Rapiejko PJ, Gilmore R. 1991. Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor. Science 252: 1171-1173.
    • (1991) Science , vol.252 , pp. 1171-1173
    • Connolly, T.1    Rapiejko, P.J.2    Gilmore, R.3
  • 24
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley KS, Reinhart GD, Johnson AE. 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
  • 25
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum via an aqueous, gated pore
    • Crowley KS, Liao S, Worrell VE, Reinhart GD, Johnson AE. 1994. Secretory proteins move through the endoplasmic reticulum 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
  • 26
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies RJ, Schekman R. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J Cell Biol 105: 633-645.
    • (1987) J Cell Biol , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 27
    • 0024828302 scopus 로고
    • Sec62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum
    • Deshaies RJ, Schekman R. 1989. Sec62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum. J Cell Biol 109: 2653-2664.
    • (1989) J Cell Biol , vol.109 , pp. 2653-2664
    • Deshaies, R.J.1    Schekman, R.2
  • 28
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies RJ, Koch BD, Werner-Washburne M, Craig EA, Schekman R. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332: 800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 29
    • 0025970051 scopus 로고
    • Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • Deshaies RJ, Sanders SL, Feldheim DA, Schekman R. 1991. Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature 349: 806-808.
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.A.3    Schekman, R.4
  • 30
    • 0034020622 scopus 로고    scopus 로고
    • Largescale identification of secreted and membrane-associated gene products using DNA microarrays
    • Diehn M, Eisen MB, Botstein D, Brown PO. 2000. Largescale identification of secreted and membrane-associated gene products using DNA microarrays. Nat Genet 25: 58-62.
    • (2000) Nat Genet , vol.25 , pp. 58-62
    • Diehn, M.1    Eisen, M.B.2    Botstein, D.3    Brown, P.O.4
  • 31
    • 78049253482 scopus 로고    scopus 로고
    • Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
    • Egea PF, Stroud RM. 2010. Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci 107: 17182-17187.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 17182-17187
    • Egea, P.F.1    Stroud, R.M.2
  • 33
    • 0027520458 scopus 로고
    • The yeast SSS1 gene is essential for secretory protein translocation and encodes aconserved protein of the endoplasmic reticulum
    • Esnault Y, Blondel M-O, Deshaies R, Schekman R, Képes F. 1993. The yeast SSS1 gene is essential for secretory protein translocation and encodes aconserved protein of the endoplasmic reticulum. EMBO J 12: 4083-4093.
    • (1993) EMBO J , vol.12 , pp. 4083-4093
    • Esnault, Y.1    Blondel, M.-O.2    Deshaies, R.3    Schekman, R.4    Képes, F.5
  • 34
    • 0028151096 scopus 로고
    • SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus
    • Esnault Y, Feldheim D, Blondel M-O, Schekman R, Képes F. 1994. SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J Biol Chem 269: 27478-27485.
    • (1994) J Biol Chem , vol.269 , pp. 27478-27485
    • Esnault, Y.1    Feldheim, D.2    Blondel, M.-O.3    Schekman, R.4    Képes, F.5
  • 35
    • 0028088419 scopus 로고
    • Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p- BiP complex from S. cerevisiae
    • Fang H, Green N. 1994. Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p- BiP complex from S. cerevisiae. Mol Biol Cell 5: 933-942.
    • (1994) Mol Biol Cell , vol.5 , pp. 933-942
    • Fang, H.1    Green, N.2
  • 36
    • 0028022701 scopus 로고
    • Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim D, Schekman R. 1994. Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J Cell Biol 126: 935-943.
    • (1994) J Cell Biol , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 37
    • 0026690820 scopus 로고
    • Topology and functional domains ofSec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
    • Feldheim D, Rothblatt J, Schekman R. 1992. Topology and functional domains ofSec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol Cell Biol 12: 3288-3296.
    • (1992) Mol Cell Biol , vol.12 , pp. 3288-3296
    • Feldheim, D.1    Rothblatt, J.2    Schekman, R.3
  • 38
    • 0027507707 scopus 로고
    • Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in yeast endoplasmic reticulum
    • Feldheim DA, Yoshimura K, Admon A, Schekman R. 1993. Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in yeast endoplasmic reticulum. Mol Biol Cell 4: 931-939.
    • (1993) Mol Biol Cell , vol.4 , pp. 931-939
    • Feldheim, D.A.1    Yoshimura, K.2    Admon, A.3    Schekman, R.4
  • 39
    • 0029881380 scopus 로고    scopus 로고
    • A second trimeric complex containing homologues of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae
    • Finke K, Plath K, Panzer S, Prehn S, Rapoport TA, Hartmann E, Sommer T. 1996. A second trimeric complex containing homologues of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15: 1482-1494.
    • (1996) EMBO J , vol.15 , pp. 1482-1494
    • Finke, K.1    Plath, K.2    Panzer, S.3    Prehn, S.4    Rapoport, T.A.5    Hartmann, E.6    Sommer, T.7
  • 41
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • Fons RD, Bogert BA, Hegde RS. 2003. Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J Cell Biol 160: 529-539.
    • (2003) J Cell Biol , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 42
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • Freymann DM, Keenan RJ, Stroud RM, Walter P. 1997. Structure of the conserved GTPase domain of the signal recognition particle. Nature 385: 361-364.
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 44
    • 0022358406 scopus 로고
    • Bovine opsin has more than one signal sequence
    • Friedlander M, Blobel G. 1985. Bovine opsin has more than one signal sequence. Nature 318: 338-343.
    • (1985) Nature , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 45
    • 0021014636 scopus 로고
    • Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation
    • Gilmore R, Blobel G. 1983. Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation. Cell 35: 677-685.
    • (1983) Cell , vol.35 , pp. 677-685
    • Gilmore, R.1    Blobel, G.2
  • 46
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore R, Blobel G. 1985. Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42: 497-505.
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 47
    • 0020357598 scopus 로고
    • Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
    • Gilmore R, Blobel G, Walter P. 1982a. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J Cell Biol 95: 463-469.
    • (1982) J Cell Biol , vol.95 , pp. 463-469
    • Gilmore, R.1    Blobel, G.2    Walter, P.3
  • 48
    • 0020413603 scopus 로고
    • Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
    • Gilmore R, Walter P, Blobel G. 1982b. Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol 95: 470-477.
    • (1982) J Cell Biol , vol.95 , pp. 470-477
    • Gilmore, R.1    Walter, P.2    Blobel, G.3
  • 49
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the ER membrane
    • Görlich D, Rapoport TA. 1993. Protein translocation into proteoliposomes reconstituted from purified components of the ER membrane. Cell 75: 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 50
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich D, Hartmann E, Prehn S, Rapoport T. 1992a. 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.4
  • 51
    • 0026466143 scopus 로고
    • A mammalian homologue of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich D, Prehn S, Hartmann E, Kalies K-U, Rapoport TA. 1992b. A mammalian homologue 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
  • 52
    • 0026531641 scopus 로고
    • Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae
    • Green N, Fang H, Walter P. 1992. Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J Cell Biol 116: 597-604.
    • (1992) J Cell Biol , vol.116 , pp. 597-604
    • Green, N.1    Fang, H.2    Walter, P.3
  • 53
    • 34848895197 scopus 로고    scopus 로고
    • Structural determinants of lateral gate opening in the protein translocon
    • Gumbart J, Schulten K. 2007. Structural determinants of lateral gate opening in the protein translocon. Biochemistry 46: 11147-11157.
    • (2007) Biochemistry , vol.46 , pp. 11147-11157
    • Gumbart, J.1    Schulten, K.2
  • 54
    • 3242892326 scopus 로고    scopus 로고
    • Protein transport into canine pancreatic microsomes: A quantitative approach
    • Guth S, Volzing C, Muller A, Jung M, Zimmermann R. 2004. Protein transport into canine pancreatic microsomes: A quantitative approach. Eur J Biochem 271: 3200-3207.
    • (2004) Eur J Biochem , vol.271 , pp. 3200-3207
    • Guth, S.1    Volzing, C.2    Muller, A.3    Jung, M.4    Zimmermann, R.5
  • 55
    • 0037148535 scopus 로고    scopus 로고
    • A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane
    • Haigh NG, Johnson AE. 2002. A new role for BiP: Closing the aqueous translocon pore during protein integration into the ER membrane. J Cell Biol 156: 261-270.
    • (2002) J Cell Biol , vol.156 , pp. 261-270
    • Haigh, N.G.1    Johnson, A.E.2
  • 56
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M, Becker T, Pool MR, Spahn CM, Grassucci RA, Frank J, Beckmann R. 2004. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427: 808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 57
    • 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 BD, Chen J-C, Johnson EE, Johnson AE. 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
  • 58
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation
    • Hamman BD, Hendershot LM, Johnson AE. 1998. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation. Cell 92: 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 60
    • 0025949923 scopus 로고
    • The signal recognition particle in S. cerevisiae
    • Hann BC, Walter P. 1991. The signal recognition particle in S. cerevisiae. Cell 67: 131-144.
    • (1991) Cell , vol.67 , pp. 131-144
    • Hann, B.C.1    Walter, P.2
  • 61
    • 0023045298 scopus 로고
    • In vitro protein translocation across the yeast endoplasmic reticulum. ATPdependent posttranslational translocation of the prepro-a-factor
    • Hansen W, Garcia PD, Walter P. 1986. In vitro protein translocation across the yeast endoplasmic reticulum. ATPdependent posttranslational translocation of the prepro-a-factor. Cell 45: 397-406.
    • (1986) Cell , vol.45 , pp. 397-406
    • Hansen, W.1    Garcia, P.D.2    Walter, P.3
  • 62
    • 78951489755 scopus 로고    scopus 로고
    • Structural studies and the assembly of the heptameric post-translational translocon complex
    • Harada Y, Li H, Wall JS, Lennarz WJ. 2011. Structural studies and the assembly of the heptameric post-translational translocon complex. J Biol Chem 286: 2956-2965.
    • (2011) J Biol Chem , vol.286 , pp. 2956-2965
    • Harada, Y.1    Li, H.2    Wall, J.S.3    Lennarz, W.J.4
  • 63
    • 0032489505 scopus 로고    scopus 로고
    • TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum
    • Hegde RS, Voigt S, Rapoport TA, Lingappa VR. 1998. TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum. Cell 92: 621-631.
    • (1998) Cell , vol.92 , pp. 621-631
    • Hegde, R.S.1    Voigt, S.2    Rapoport, T.A.3    Lingappa, V.R.4
  • 64
    • 33646361833 scopus 로고    scopus 로고
    • The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons
    • Jermy AJ, Willer M, Davis E, Wilkinson BM, Stirling CJ. 2006. The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons. J Biol Chem 281: 7899-7906.
    • (2006) J Biol Chem , vol.281 , pp. 7899-7906
    • Jermy, A.J.1    Willer, M.2    Davis, E.3    Wilkinson, B.M.4    Stirling, C.J.5
  • 65
    • 41549097803 scopus 로고    scopus 로고
    • An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation
    • Jiang Y, Cheng Z, Mandon EC, Gilmore R. 2008. An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation. J Cell Biol 180: 1149-1161.
    • (2008) J Cell Biol , vol.180 , pp. 1149-1161
    • Jiang, Y.1    Cheng, Z.2    Mandon, E.C.3    Gilmore, R.4
  • 66
    • 33748300566 scopus 로고    scopus 로고
    • The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability
    • Junne T, Schwede T, Goder V, Spiess M. 2006. The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability. Mol Biol Cell 17: 4063-4068.
    • (2006) Mol Biol Cell , vol.17 , pp. 4063-4068
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 67
    • 36349034451 scopus 로고    scopus 로고
    • Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology
    • Junne T, Schwede T, Goder V, Spiess M. 2007. Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. J Biol Chem 282: 33201-33209.
    • (2007) J Biol Chem , vol.282 , pp. 33201-33209
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 68
    • 77952378779 scopus 로고    scopus 로고
    • The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration
    • Junne T, Kocik L, Spiess M. 2010. The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration. Mol Biol Cell 21: 1662-1670.
    • (2010) Mol Biol Cell , vol.21 , pp. 1662-1670
    • Junne, T.1    Kocik, L.2    Spiess, M.3
  • 69
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum is mediated by the Sec61p-complex
    • Kalies K-U, Görlich D, Rapoport TA. 1994. Binding of ribosomes to the rough endoplasmic reticulum is mediated by the Sec61p-complex. J Cell Biol 126: 925-934.
    • (1994) J Cell Biol , vol.126 , pp. 925-934
    • Kalies, K.-U.1    Görlich, D.2    Rapoport, T.A.3
  • 70
    • 0026092029 scopus 로고
    • ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein
    • Kellaris KV, Bowen S, Gilmore R. 1991. ER translocation intermediates are adjacent to a nonglycosylated 34-kD integral membrane protein. J Cell Biol 114: 21-33.
    • (1991) J Cell Biol , vol.114 , pp. 21-33
    • Kellaris, K.V.1    Bowen, S.2    Gilmore, R.3
  • 71
    • 0032816265 scopus 로고    scopus 로고
    • In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/ SecB as constituents of two independent protein-targeting pathways of Escherichia coli
    • Koch HG, Hengelage T, Neumann-Haefelin C, MacFarlane J, Hoffschulte HK, Schimz KL, Mechler B, Muller M. 1999. In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/ SecB as constituents of two independent protein-targeting pathways of Escherichia coli. Mol Biol Cell 10: 2163-2173.
    • (1999) Mol Biol Cell , vol.10 , pp. 2163-2173
    • Koch, H.G.1    Hengelage, T.2    Neumann-Haefelin, C.3    Macfarlane, J.4    Hoffschulte, H.K.5    Schimz, K.L.6    Mechler, B.7    Muller, M.8
  • 72
    • 42949161206 scopus 로고    scopus 로고
    • SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites
    • Lakkaraju AK, Mary C, Scherrer A, Johnson AE, Strub K. 2008. SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell 133: 440-451.
    • (2008) Cell , vol.133 , pp. 440-451
    • Lakkaraju, A.K.1    Mary, C.2    Scherrer, A.3    Johnson, A.E.4    Strub, K.5
  • 74
    • 0022357545 scopus 로고
    • Topology of signal recognition particle receptor in endoplasmic reticulum membrane
    • Lauffer L, Garcia PD, Harkins RN, Coussens L, Ullrich A, Walter P. 1985. Topology of signal recognition particle receptor in endoplasmic reticulum membrane. Nature 318: 334-338.
    • (1985) Nature , vol.318 , pp. 334-338
    • Lauffer, L.1    Garcia, P.D.2    Harkins, R.N.3    Coussens, L.4    Ullrich, A.5    Walter, P.6
  • 75
    • 0034282447 scopus 로고    scopus 로고
    • Nucleotidedependent binding of the GTPase domain of the signal recognition particle receptor b-subunit to the a-subunit
    • Legate KR, Falcone D, Andrews DW. 2000. Nucleotidedependent binding of the GTPase domain of the signal recognition particle receptor b-subunit to the a-subunit. J Biol Chem 275: 27439-27446.
    • (2000) J Biol Chem , vol.275 , pp. 27439-27446
    • Legate, K.R.1    Falcone, D.2    Andrews, D.W.3
  • 77
    • 0028809495 scopus 로고
    • Interaction between BiP and Sec63 is required for the completion of protein translocation across the ER of Saccharomyces cerevisiae
    • Lyman SK, Schekman R. 1995. Interaction between BiP and Sec63 is required for the completion of protein translocation across the ER of Saccharomyces cerevisiae. J Cell Biol 131: 1163-1171.
    • (1995) J Cell Biol , vol.131 , pp. 1163-1171
    • Lyman, S.K.1    Schekman, R.2
  • 78
    • 33847698213 scopus 로고    scopus 로고
    • Deregulation of the SecYEG translocation channel upon removal of the plug domain
    • Maillard AP, Lalani S, Silva F, Belin D, Duong F. 2007. Deregulation of the SecYEG translocation channel upon removal of the plug domain. J Biol Chem 282: 1281-1287.
    • (2007) J Biol Chem , vol.282 , pp. 1281-1287
    • Maillard, A.P.1    Lalani, S.2    Silva, F.3    Belin, D.4    Duong, F.5
  • 79
    • 0041977048 scopus 로고    scopus 로고
    • Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum
    • Mandon EC, Jiang Y, Gilmore R. 2003. Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum. J Cell Biol 162: 575-585.
    • (2003) J Cell Biol , vol.162 , pp. 575-585
    • Mandon, E.C.1    Jiang, Y.2    Gilmore, R.3
  • 80
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason N, Ciufo LF, Brown JD. 2000. Elongation arrest is a physiologically important function of signal recognition particle. EMBO J 19: 4164-4174.
    • (2000) EMBO J , vol.19 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 81
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts asa molecular ratchet during posttranslational transport of prepro-a factor across the ER membrane
    • Matlack KE, Misselwitz B, Plath K, Rapoport TA. 1999. BiP acts asa molecular ratchet during posttranslational transport of prepro-a factor across the ER membrane. Cell 97: 553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 85
    • 0027433308 scopus 로고
    • GTP binding and hydrolysis by the signal recognition particle during initiation of protein translocation
    • Miller JD, 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
  • 86
    • 0028158717 scopus 로고
    • Interaction ofE. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
    • Miller JD, Bernstein HD, Walter P. 1994. Interaction ofE. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor. Nature 367: 657-659.
    • (1994) Nature , vol.367 , pp. 657-659
    • Miller, J.D.1    Bernstein, H.D.2    Walter, P.3
  • 88
    • 0022878780 scopus 로고
    • A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum
    • Mize NK, Andrews DW, Lingappa VR. 1986. A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum. Cell 47: 711-719.
    • (1986) Cell , vol.47 , pp. 711-719
    • Mize, N.K.1    Andrews, D.W.2    Lingappa, V.R.3
  • 89
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal recognition particle receptor FtsY
    • Montoya G, Svensson C, Luirink J, Sinning I. 1997. Crystal structure of the NG domain from the signal recognition particle receptor FtsY. Nature 385: 365-368.
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 90
    • 0036927080 scopus 로고    scopus 로고
    • Structure of the mammalian ribo ° some-channel complex at 17 A resolution
    • Morgan DG, Menetret JF, Neuhof A, Rapoport TA, Akey CW. 2002. Structure of the mammalian ribo ° some-channel complex at 17 A resolution. J Mol Biol 324: 871-886.
    • (2002) J Mol Biol , vol.324 , pp. 871-886
    • Morgan, D.G.1    Menetret, J.F.2    Neuhof, A.3    Rapoport, T.A.4    Akey, C.W.5
  • 91
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes W, Prehn S, Rapoport TA. 1994. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J 13: 3973-3982.
    • (1994) EMBO J , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 92
    • 0037993062 scopus 로고
    • Import of honeybee prepromelittin into the endoplasmic reticulum: Structural basis for independence of SRP and docking protein
    • Muller G, Zimmermann R. 1987. Import of honeybee prepromelittin into the endoplasmic reticulum: Structural basis for independence of SRP and docking protein. EMBO J 6: 2099-2107.
    • (1987) EMBO J , vol.6 , pp. 2099-2107
    • Muller, G.1    Zimmermann, R.2
  • 93
    • 0026528370 scopus 로고
    • Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane
    • Müsch A, Wiedmann M, Rapoport TA. 1992. Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. Cell 69: 343-352.
    • (1992) Cell , vol.69 , pp. 343-352
    • Müsch, A.1    Wiedmann, M.2    Rapoport, T.A.3
  • 94
    • 0030051440 scopus 로고    scopus 로고
    • ER membrane protein complex required for nuclear fusion
    • Ng DTW, Walter P. 1996. ER membrane protein complex required for nuclear fusion. J Cell Biol 132: 499-509.
    • (1996) J Cell Biol , vol.132 , pp. 499-509
    • Ng, D.T.W.1    Walter, P.2
  • 95
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum
    • Ng DTW, Brown JD, Walter P. 1996. Signal sequences specify the targeting route to the endoplasmic reticulum. J Cell Biol 134: 269-278.
    • (1996) J Cell Biol , vol.134 , pp. 269-278
    • Ng, D.T.W.1    Brown, J.D.2    Walter, P.3
  • 96
    • 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 SW, Kato Y, Brodsky JL, Endo T. 2001. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153: 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
  • 97
    • 0027057308 scopus 로고
    • Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae
    • Ogg SC, Poritz MA, Walter P. 1992. Signal recognition particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol Biol Cell 3: 895-911.
    • (1992) Mol Biol Cell , vol.3 , pp. 895-911
    • Ogg, S.C.1    Poritz, M.A.2    Walter, P.3
  • 98
    • 0032572527 scopus 로고    scopus 로고
    • A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor b-subunit
    • Ogg SC, Barz WP, Walter P. 1998. A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor b-subunit. J Cell Biol 142: 341-354.
    • (1998) J Cell Biol , vol.142 , pp. 341-354
    • Ogg, S.C.1    Barz, W.P.2    Walter, P.3
  • 99
    • 0002443434 scopus 로고
    • A small particulate component of the cytoplasm
    • Palade GE. 1955a. A small particulate component of the cytoplasm. J Biophys Biochem Cytol 1: 59-68.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 59-68
    • Palade, G.E.1
  • 100
    • 0008759930 scopus 로고
    • Studies on the endoplasmic reticulum. II. Simple dispositions in cells in situ
    • Palade GE. 1955b. Studies on the endoplasmic reticulum. II. Simple dispositions in cells in situ. J Biophys Biochem Cytol 1: 567-582.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 567-582
    • Palade, G.E.1
  • 101
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport TA. 1995. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81: 561-570.
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 102
    • 79955901001 scopus 로고    scopus 로고
    • Preserving the membrane barrier for small molecules during bacterial protein translocation
    • Park E, Rapoport TA. 2011. Preserving the membrane barrier for small molecules during bacterial protein translocation. Nature 473: 239-242.
    • (2011) Nature , vol.473 , pp. 239-242
    • Park, E.1    Rapoport, T.A.2
  • 103
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecYmediated protein translocation across membranes
    • Park E, Rapoport TA. 2012. Mechanisms of Sec61/SecYmediated protein translocation across membranes. Annu Rev Biophys 41: 21-40.
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 104
    • 0034596007 scopus 로고    scopus 로고
    • Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor
    • Peluso P, Herschlag D, Nock S, Freymann DM, Johnson AE, Walter P. 2000. Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor. Science 288: 1640-1643.
    • (2000) Science , vol.288 , pp. 1640-1643
    • Peluso, P.1    Herschlag, D.2    Nock, S.3    Freymann, D.M.4    Johnson, A.E.5    Walter, P.6
  • 105
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA. 1998. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94: 795-807.
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 106
    • 0024280925 scopus 로고
    • Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain
    • Poritz MA, Strub K, Walter P. 1988. Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain. Cell 55: 4-6.
    • (1988) Cell , vol.55 , pp. 4-6
    • Poritz, M.A.1    Strub, K.2    Walter, P.3
  • 107
    • 0025605808 scopus 로고
    • An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
    • Poritz MA, Bernstein HD, Strub K, Zopf D, Wilhelm H, Walter P. 1990. An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle. Science 250: 1111-1117.
    • (1990) Science , vol.250 , pp. 1111-1117
    • Poritz, M.A.1    Bernstein, H.D.2    Strub, K.3    Zopf, D.4    Wilhelm, H.5    Walter, P.6
  • 108
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • Powers T, Walter P. 1995. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 269: 1422-1424.
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 109
    • 0033787091 scopus 로고    scopus 로고
    • Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae
    • Prinz A, Hartmann E, Kalies KU. 2000. Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae. Biol Chem 381: 1025-1029.
    • (2000) Biol Chem , vol.381 , pp. 1025-1029
    • Prinz, A.1    Hartmann, E.2    Kalies, K.U.3
  • 110
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequenceand translation-independent mRNA localization to the endoplasmic reticulum
    • Pyhtila B, Zheng T, Lager PJ, Keene JD, Reedy MC, Nicchitta CV. 2008. Signal sequenceand translation-independent mRNA localization to the endoplasmic reticulum. RNA 14: 445-453.
    • (2008) RNA , vol.14 , pp. 445-453
    • Pyhtila, B.1    Zheng, T.2    Lager, P.J.3    Keene, J.D.4    Reedy, M.C.5    Nicchitta, C.V.6
  • 111
    • 0034631835 scopus 로고    scopus 로고
    • Role of the cytoplasmic segments of Sec61a in the ribosome-binding and translocation-promoting activities ofthe Sec61 complex
    • Raden D, Song W, Gilmore R. 2000. Role of the cytoplasmic segments of Sec61a in the ribosome-binding and translocation-promoting activities ofthe Sec61 complex. J Cell Biol 150: 53-64.
    • (2000) J Cell Biol , vol.150 , pp. 53-64
    • Raden, D.1    Song, W.2    Gilmore, R.3
  • 112
    • 0017256005 scopus 로고
    • A procedure for the quantitative recovery of homogenous populations of undegraded free and bound polysomes from rat liver
    • Ramsey JC, Steele WJ. 1976. A procedure for the quantitative recovery of homogenous populations of undegraded free and bound polysomes from rat liver. Biochemistry 15: 1704-1712.
    • (1976) Biochemistry , vol.15 , pp. 1704-1712
    • Ramsey, J.C.1    Steele, W.J.2
  • 113
    • 0030678106 scopus 로고    scopus 로고
    • Empty site forms of the SRP54 and SR a GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum
    • Rapiejko PJ, Gilmore R. 1997. Empty site forms of the SRP54 and SR a GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum. Cell 89: 703-713.
    • (1997) Cell , vol.89 , pp. 703-713
    • Rapiejko, P.J.1    Gilmore, R.2
  • 114
    • 0013936848 scopus 로고
    • Vectorial discharge of peptides released by puromycin from attached ribosomes
    • Redman C, Sabatini DD. 1966. Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc Natl Acad Sci 56: 608-615.
    • (1966) Proc Natl Acad Sci , vol.56 , pp. 608-615
    • Redman, C.1    Sabatini, D.D.2
  • 115
    • 0014010396 scopus 로고
    • Synthesis and transfer of amylase in pigeon pancreatic microsomes
    • Redman C, Siekevitz P, Palade GE. 1966. Synthesis and transfer of amylase in pigeon pancreatic microsomes. J Biol Chem 241: 1150-1158.
    • (1966) J Biol Chem , vol.241 , pp. 1150-1158
    • Redman, C.1    Siekevitz, P.2    Palade, G.E.3
  • 116
    • 0344304454 scopus 로고    scopus 로고
    • Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    • Rosendal KR, Wild K, Montoya G, Sinning I. 2003. Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication. Proc Natl Acad Sci 100: 14701-14706.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 14701-14706
    • Rosendal, K.R.1    Wild, K.2    Montoya, G.3    Sinning, I.4
  • 117
    • 0012304561 scopus 로고
    • Secretion in yeast: Translocation and glycosylation of prepro-a-factor in vitro can occur via an ATP-dependent post-translational mechanism
    • Rothblatt JA, Meyer DI. 1986. Secretion in yeast: Translocation and glycosylation of prepro-a-factor in vitro can occur via an ATP-dependent post-translational mechanism. EMBO J 5: 1031-1036.
    • (1986) EMBO J , vol.5 , pp. 1031-1036
    • Rothblatt, J.A.1    Meyer, D.I.2
  • 118
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt JA, Deshaies RJ, Sanders SL, Daum G, Schekman R. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J Cell Biol 109: 2641-2652.
    • (1989) J Cell Biol , vol.109 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 119
    • 0026589260 scopus 로고
    • Sec61p and Bip directly facilitate polypeptide translocation into the ER
    • Sanders SL, Whitfield KM, Vogel JP, Rose MD, Schekman RW. 1992. Sec61p and Bip directly facilitate polypeptide translocation into the ER. Cell 69: 353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 121
    • 0023305012 scopus 로고
    • Import of frog prepropeptide GLa into microsomes requires ATP but does not involve docking protein or ribosomes
    • Schlenstedt G, Zimmermann R. 1987. Import of frog prepropeptide GLa into microsomes requires ATP but does not involve docking protein or ribosomes. EMBO J 6: 699-703.
    • (1987) EMBO J , vol.6 , pp. 699-703
    • Schlenstedt, G.1    Zimmermann, R.2
  • 122
    • 0037459447 scopus 로고    scopus 로고
    • Structural basis for the function of the b subunit of the eukaryotic signal recognition particle receptor
    • Schwartz T, Blobel G. 2003. Structural basis for the function of the b subunit of the eukaryotic signal recognition particle receptor. Cell 112: 793-803.
    • (2003) Cell , vol.112 , pp. 793-803
    • Schwartz, T.1    Blobel, G.2
  • 123
    • 0037447254 scopus 로고    scopus 로고
    • Induced nucleotide specificity in a GTPase
    • Shan SO, Walter P. 2003. Induced nucleotide specificity in a GTPase. Proc Natl Acad Sci 100: 4480-4485.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 4480-4485
    • Shan, S.O.1    Walter, P.2
  • 124
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao S, Hegde RS. 2011. Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol 27: 25-56.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 125
    • 84455178968 scopus 로고    scopus 로고
    • A calmodulin-dependent translocation pathway for small secretory proteins
    • Shao S, Hegde RS. 2012. A calmodulin-dependent translocation pathway for small secretory proteins. Cell 147: 1576-1588.
    • (2012) Cell , vol.147 , pp. 1576-1588
    • Shao, S.1    Hegde, R.S.2
  • 126
    • 0024121564 scopus 로고
    • Binding sites of the 19-kDa and 68/ 72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined by protein-RNA footprinting
    • Siegel V, Walter P. 1988. Binding sites of the 19-kDa and 68/ 72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined by protein-RNA "footprinting." Proc Natl Acad Sci 85: 1801-1805.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 1801-1805
    • Siegel, V.1    Walter, P.2
  • 127
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon SM, 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
  • 128
    • 24944465005 scopus 로고    scopus 로고
    • Modeling the effects of prl mutations on the Escherichia coli SecY complex
    • Smith MA, Clemons WM Jr, DeMars CJ, Flower AM. 2005. Modeling the effects of prl mutations on the Escherichia coli SecY complex. J Bacteriol 187: 6454-6465.
    • (2005) J Bacteriol , vol.187 , pp. 6454-6465
    • Smith, M.A.1    Clemons Jr., W.M.2    Demars, C.J.3    Flower, A.M.4
  • 129
    • 0034602866 scopus 로고    scopus 로고
    • Role of Sec61ain the regulated transferof the ribosome-nascent chain complex from the signal recognition particle to the translocation channel
    • Song W, Raden D, Mandon EC, Gilmore R. 2000. Role of Sec61ain the regulated transferof the ribosome-nascent chain complex from the signal recognition particle to the translocation channel. Cell 100: 333-343.
    • (2000) Cell , vol.100 , pp. 333-343
    • Song, W.1    Raden, D.2    Mandon, E.C.3    Gilmore, R.4
  • 130
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling CJ, Rothblatt J, Hosobuchi M, Deshaies R, Schekman R. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol Biol Cell 3: 129-142.
    • (1992) Mol Biol Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 131
    • 0025098763 scopus 로고
    • Assembly of the Alu domain of the signal recognition particle (SRP): Dimerization of the two protein components is required for efficient binding to SRP RNA
    • Strub K, Walter P. 1990. Assembly of the Alu domain of the signal recognition particle (SRP): Dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Cell Biol 10: 777-784.
    • (1990) Mol Cell Biol , vol.10 , pp. 777-784
    • Strub, K.1    Walter, P.2
  • 132
    • 80052237952 scopus 로고    scopus 로고
    • Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity
    • Trueman SF, Mandon EC, Gilmore R. 2011. Translocation channel gating kinetics balances protein translocation efficiency with signal sequence recognition fidelity. Mol Biol Cell 22: 2983-2993.
    • (2011) Mol Biol Cell , vol.22 , pp. 2983-2993
    • Trueman, S.F.1    Mandon, E.C.2    Gilmore, R.3
  • 135
    • 0031472242 scopus 로고    scopus 로고
    • The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins
    • Ulbrandt ND, Newitt JA, Bernstein HD. 1997. The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins. Cell 88: 187-196.
    • (1997) Cell , vol.88 , pp. 187-196
    • Ulbrandt, N.D.1    Newitt, J.A.2    Bernstein, H.D.3
  • 137
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel JP, Misra LM, Rose MD. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J Cell Biol 110: 1885-1895.
    • (1990) J Cell Biol , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 138
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum
    • Voigt S, Jungnickel B, Hartmann E, Rapoport TA. 1996. Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum. J Cell Biol 134: 25-35.
    • (1996) J Cell Biol , vol.134 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 139
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal sequence cleavage sites
    • von Heijne G. 1983. Patterns of amino acids near signal sequence cleavage sites. Eur J Biochem 133: 17-21.
    • (1983) Eur J Biochem , vol.133 , pp. 17-21
    • von Heijne, G.1
  • 140
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7: 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 141
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter P, Blobel G. 1980. Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci 77: 7112-7116.
    • (1980) Proc Natl Acad Sci , vol.77 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 142
    • 0019817924 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein
    • Walter P, Blobel G. 1981a. Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein. J Cell Biol 91: 551-556.
    • (1981) J Cell Biol , vol.91 , pp. 551-556
    • Walter, P.1    Blobel, G.2
  • 143
    • 0019822645 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence-dependent and sitespecific arrest of chain elongation that is released by microsomal membranes
    • Walter P, Blobel G. 1981b. Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence-dependent and sitespecific arrest of chain elongation that is released by microsomal membranes. J Cell Biol 91: 557-561.
    • (1981) J Cell Biol , vol.91 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 144
    • 0019964240 scopus 로고
    • Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
    • Walter P, Blobel G. 1982. Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature 299: 691-698.
    • (1982) Nature , vol.299 , pp. 691-698
    • Walter, P.1    Blobel, G.2
  • 145
    • 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
  • 146
    • 0022467725 scopus 로고
    • Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis
    • Waters MG, Blobel G. 1986. Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis. J Cell Biol 102: 1543-1550.
    • (1986) J Cell Biol , vol.102 , pp. 1543-1550
    • Waters, M.G.1    Blobel, G.2
  • 147
    • 0024807163 scopus 로고
    • Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum
    • Wiedmann M, Goerlich D, Hartmann E, Kurzchalia TV, Rapoport TA. 1989. Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum. FEBS Lett 257: 263-268.
    • (1989) FEBS Lett , vol.257 , pp. 263-268
    • Wiedmann, M.1    Goerlich, D.2    Hartmann, E.3    Kurzchalia, T.V.4    Rapoport, T.A.5
  • 148
    • 0038470026 scopus 로고    scopus 로고
    • An in vitro assay using overexpressed yeast SRP demonstrates that cotranslational translocation is dependent upon the J-domain of Sec63p
    • Willer M, Jermy AJ, Steel GJ, Garside HJ, Carter S, Stirling CJ. 2003. An in vitro assay using overexpressed yeast SRP demonstrates that cotranslational translocation is dependent upon the J-domain of Sec63p. Biochemistry 42: 7171-7177.
    • (2003) Biochemistry , vol.42 , pp. 7171-7177
    • Willer, M.1    Jermy, A.J.2    Steel, G.J.3    Garside, H.J.4    Carter, S.5    Stirling, C.J.6
  • 149
    • 0033738377 scopus 로고    scopus 로고
    • Sec62p, A component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the sec-complex
    • Wittke S, Dunnwald M, Johnsson N. 2000. Sec62p, A component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the sec-complex. Mol Biol Cell 11: 3859-3871.
    • (2000) Mol Biol Cell , vol.11 , pp. 3859-3871
    • Wittke, S.1    Dunnwald, M.2    Johnsson, N.3
  • 150
    • 0036322966 scopus 로고    scopus 로고
    • Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae
    • Wittke S, Dunnwald M, Albertsen M, Johnsson N. 2002. Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae. Mol Biol Cell 13: 2223-2232.
    • (2002) Mol Biol Cell , vol.13 , pp. 2223-2232
    • Wittke, S.1    Dunnwald, M.2    Albertsen, M.3    Johnsson, N.4
  • 151
    • 0035862963 scopus 로고    scopus 로고
    • Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo
    • Young BP, Craven RA, Reid PJ, Willer M, Stirling CJ. 2001. Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20: 262-271.
    • (2001) EMBO J , vol.20 , pp. 262-271
    • Young, B.P.1    Craven, R.A.2    Reid, P.J.3    Willer, M.4    Stirling, C.J.5
  • 152
    • 77952127782 scopus 로고    scopus 로고
    • Sequential checkpoints govern substrate selection during cotranslational protein targeting
    • Zhang X, Rashid R, Wang K, Shan SO. 2010. Sequential checkpoints govern substrate selection during cotranslational protein targeting. Science 328: 757-760.
    • (2010) Science , vol.328 , pp. 757-760
    • Zhang, X.1    Rashid, R.2    Wang, K.3    Shan, S.O.4
  • 153
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the protein-translocation channel
    • Zimmer J, Nam Y, Rapoport TA. 2008. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455: 936-943.
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1    Nam, Y.2    Rapoport, T.A.3
  • 154
    • 0025601549 scopus 로고
    • The methionine-rich domain of the 54 kD protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence
    • Zopf D, Bernstein HD, Johnson AE, Walter P. 1990. The methionine-rich domain of the 54 kD protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 9: 4511-4517.
    • (1990) EMBO J , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4


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