메뉴 건너뛰기




Volumn 21, Issue 3, 2010, Pages 418-429

Environmental transition of signal-anchor sequences during membrane insertion via the endoplasmic reticulum translocon

Author keywords

[No Author keywords available]

Indexed keywords

TRANSLOCON;

EID: 76049128995     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-08-0738     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 48449091228 scopus 로고    scopus 로고
    • Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface
    • Alder, N. N., Jensen, R. E., and Johnson, A. E. (2008). Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface. Cell 134, 439-450.
    • (2008) Cell , vol.134 , pp. 439-450
    • Alder, N.N.1    Jensen, R.E.2    Johnson, A.E.3
  • 2
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex
    • Beckmann, R., Bubeck, D., Grassucci, R., Penczek, P., Verschoor, A., Blobel, G., and Frank, J. (1997). Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278, 2123-2126.
    • (1997) Science , vol.278 , pp. 2123-2126
    • Beckmann, R.1    Bubeck, D.2    Grassucci, R.3    Penczek, P.4    Verschoor, A.5    Blobel, G.6    Frank, J.7
  • 3
    • 65249159700 scopus 로고    scopus 로고
    • Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins
    • Boy, D., and Koch, H. G. (2009). Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins. Mol. Biol. Cell 20, 1804-1815.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1804-1815
    • Boy, D.1    Koch, H.G.2
  • 4
    • 33845307248 scopus 로고    scopus 로고
    • Unassisted translocation of large polypeptide domains across phospholipid bilayers
    • Brambillasca, S., Yabal, M., Makarow, M., and Borgese, N. (2006). Unassisted translocation of large polypeptide domains across phospholipid bilayers. J. Cell Biol. 175, 767-777.
    • (2006) J. Cell Biol , vol.175 , pp. 767-777
    • Brambillasca, S.1    Yabal, M.2    Makarow, M.3    Borgese, N.4
  • 5
    • 18544380083 scopus 로고    scopus 로고
    • Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
    • Cannon, K. S., Or, E., Clemons, W. M., Jr., Shibata, Y., and Rapoport, T. A. (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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: Determinants and dynamics
    • Goder, V., and Spiess, M. (2001). Topogenesis of membrane proteins: determinants and dynamics. FEBS Lett. 504, 87-93.
    • (2001) FEBS Lett , vol.504 , pp. 87-93
    • Goder, V.1    Spiess, M.2
  • 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
  • 10
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B. D., Hendershot, L. M., and Johnson, A. E. (1998). BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 12
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich, S. U., Mothes, W., Brunner, J., and Rapoport, T. A. (2000). The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102, 233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 13
    • 0042815085 scopus 로고    scopus 로고
    • Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane
    • Heinrich, S. U., and Rapoport, T. A. (2003). Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane. EMBO J. 22, 3654-3663.
    • (2003) EMBO J , vol.22 , pp. 3654-3663
    • Heinrich, S.U.1    Rapoport, T.A.2
  • 16
    • 0021004695 scopus 로고
    • Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA
    • Jackson, R. J., and Hunt, T. (1983). Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96, 50-74.
    • (1983) Methods Enzymol , vol.96 , pp. 50-74
    • Jackson, R.J.1    Hunt, T.2
  • 17
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • Johnson, A. E., and van Waes, M. A. (1999). The translocon: a dynamic gateway at the ER membrane. Annu. Rev. Cell Dev. Biol. 15, 799-842.
    • (1999) Annu. Rev. Cell Dev. Biol , vol.15 , pp. 799-842
    • Johnson, A.E.1    van Waes, M.A.2
  • 18
    • 25144519777 scopus 로고    scopus 로고
    • Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence
    • Kida, Y., Mihara, K., and Sakaguchi, M. (2005). Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence. EMBO J. 24, 3202-3213.
    • (2005) EMBO J , vol.24 , pp. 3202-3213
    • Kida, Y.1    Mihara, K.2    Sakaguchi, M.3
  • 19
    • 38049058405 scopus 로고    scopus 로고
    • Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis
    • Kida, Y., Morimoto, F., and Sakaguchi, M. (2007). Two translocating hydrophilic segments of a nascent chain span the ER membrane during multispanning protein topogenesis. J. Cell Biol. 179, 1441-1452.
    • (2007) J. Cell Biol , vol.179 , pp. 1441-1452
    • Kida, Y.1    Morimoto, F.2    Sakaguchi, M.3
  • 20
    • 59149104036 scopus 로고    scopus 로고
    • Signal anchor sequence provides motive force for polypeptide chain translocation through the endoplasmic reticulum membrane
    • Kida, Y., Morimoto, F., and Sakaguchi, M. (2009). Signal anchor sequence provides motive force for polypeptide chain translocation through the endoplasmic reticulum membrane. J. Biol. Chem. 284, 2861-2866.
    • (2009) J. Biol. Chem , vol.284 , pp. 2861-2866
    • Kida, Y.1    Morimoto, F.2    Sakaguchi, M.3
  • 21
    • 0034698758 scopus 로고    scopus 로고
    • Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum
    • Kida, Y., Sakaguchi, M., Fukuda, M., Mikoshiba, K., and Mihara, K. (2000). Membrane topogenesis of a type I signal-anchor protein, mouse synaptotagmin II, on the endoplasmic reticulum. J. Cell Biol. 150, 719-730.
    • (2000) J. Cell Biol , vol.150 , pp. 719-730
    • Kida, Y.1    Sakaguchi, M.2    Fukuda, M.3    Mikoshiba, K.4    Mihara, K.5
  • 23
    • 33947498781 scopus 로고    scopus 로고
    • Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation
    • Koide, K., Maegawa, S., Ito, K., and Akiyama, Y. (2007). Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation. J. Biol. Chem. 282, 4553-4560.
    • (2007) J. Biol. Chem , vol.282 , pp. 4553-4560
    • Koide, K.1    Maegawa, S.2    Ito, K.3    Akiyama, Y.4
  • 24
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 26
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the 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 the 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
  • 27
    • 0036906637 scopus 로고    scopus 로고
    • Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein
    • Meacock, S. L., Lecomte, F. J., Crawshaw, S. G., and High, S. (2002). Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein. Mol. Biol. Cell 13, 4114-4129.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4114-4129
    • Meacock, S.L.1    Lecomte, F.J.2    Crawshaw, S.G.3    High, S.4
  • 28
    • 46049116259 scopus 로고    scopus 로고
    • Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome
    • Menetret, J. F., Hegde, R. S., Aguiar, M., Gygi, S. P., Park, E., Rapoport, T. A., and Akey, C. W. (2008). Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome. Structure 16, 1126-1137.
    • (2008) Structure , vol.16 , pp. 1126-1137
    • Menetret, J.F.1    Hegde, R.S.2    Aguiar, M.3    Gygi, S.P.4    Park, E.5    Rapoport, T.A.6    Akey, C.W.7
  • 29
  • 30
    • 0037687309 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes
    • Mori, H., Tsukazaki, T., Masui, R., Kuramitsu, S., Yokoyama, S., Johnson, A. E., Kimura, Y., Akiyama, Y., and Ito, K. (2003). Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes. J. Biol. Chem. 278, 14257-14264.
    • (2003) J. Biol. Chem , vol.278 , pp. 14257-14264
    • Mori, H.1    Tsukazaki, T.2    Masui, R.3    Kuramitsu, S.4    Yokoyama, S.5    Johnson, A.E.6    Kimura, Y.7    Akiyama, Y.8    Ito, K.9
  • 31
  • 32
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes, W., Prehn, S., and Rapoport, T. A. (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
  • 33
    • 33947717366 scopus 로고    scopus 로고
    • Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel
    • Osborne, A. R., and Rapoport, T. A. (2007). Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell 129, 97-110.
    • (2007) Cell , vol.129 , pp. 97-110
    • Osborne, A.R.1    Rapoport, T.A.2
  • 35
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport, T. A. (2007). Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450, 663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 36
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein
    • Sadlish, H., Pitonzo, D., Johnson, A. E., and Skach, W. R. (2005). Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein. Nat. Struct. Mol. Biol. 12, 870-878.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 37
    • 0030660436 scopus 로고    scopus 로고
    • Eukaryotic protein secretion
    • Sakaguchi, M. (1997). Eukaryotic protein secretion. Curr. Opin. Biotechnol. 8, 595-601.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 595-601
    • Sakaguchi, M.1
  • 38
    • 0026675770 scopus 로고
    • Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes
    • Sakaguchi, M., Hachiya, N., Mihara, K., and Omura, T. (1992). Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes. J. Biochem. 112, 243-248.
    • (1992) J. Biochem , vol.112 , pp. 243-248
    • Sakaguchi, M.1    Hachiya, N.2    Mihara, K.3    Omura, T.4
  • 39
    • 33748297447 scopus 로고    scopus 로고
    • Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane
    • Schaletzky, J., and Rapoport, T. A. (2006). Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane. Mol. Biol. Cell 17, 3860-3869.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3860-3869
    • Schaletzky, J.1    Rapoport, T.A.2
  • 40
    • 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
  • 41
    • 54049151196 scopus 로고    scopus 로고
    • Conformational transition of Sec machinery inferred from bacterial SecYE structures
    • Tsukazaki, T., et al. (2008). Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455, 988-991.
    • (2008) Nature , vol.455 , pp. 988-991
    • Tsukazaki, T.1
  • 43
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84-93.
    • (1983) Methods Enzymol , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.