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Volumn 147, Issue 2, 1999, Pages 257-265

Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon

Author keywords

Endoplasmic reticulum; Glycosylation; Integral membrane protein; Signal recognition particle; Signal sequence

Indexed keywords

CHIMERIC PROTEIN; MEMBRANE PROTEIN; POLYPEPTIDE; SIGNAL PEPTIDE;

EID: 0032727707     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.2.257     Document Type: Article
Times cited : (81)

References (48)
  • 1
    • 0026722528 scopus 로고
    • The role of the N-region in signal sequence and signal-anchor function
    • Andrews, D.W., J.C. Young, L.F. Mirels, and G.J. Czarnota. 1992. The role of the N-region in signal sequence and signal-anchor function. J. Biol. Chem. 267:7761-7769.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7761-7769
    • Andrews, D.W.1    Young, J.C.2    Mirels, L.F.3    Czarnota, G.J.4
  • 2
    • 0025977081 scopus 로고
    • Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence
    • Beltzer, J.P., K. Fiedler, C. Fuhrer, I. Geffen, C. Handschin, H.P. Wessels, and M. Spiess. 1991. Charged residues are major determinants of the transmembrane orientation of a signal-anchor sequence. J. Biol. Chem. 266:973-978.
    • (1991) J. Biol. Chem. , vol.266 , pp. 973-978
    • Beltzer, J.P.1    Fiedler, K.2    Fuhrer, C.3    Geffen, I.4    Handschin, C.5    Wessels, H.P.6    Spiess, M.7
  • 3
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA. 77:1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 4
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both co-and posttranslational protein translocation into the yeast endoplasmic reticulum
    • Brodsky, J.L., J. Goeckeler, and R. Schekman. 1995. BiP and Sec63p are required for both co-and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 92:9643-9646.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckeler, J.2    Schekman, R.3
  • 5
    • 0022341496 scopus 로고
    • Dual functions of the signal peptide in protein transfer across the membrane
    • Coleman, J., M. Inukai, and M. Inouye. 1985. Dual functions of the signal peptide in protein transfer across the membrane. Cell. 43:351-360.
    • (1985) Cell , vol.43 , pp. 351-360
    • Coleman, J.1    Inukai, M.2    Inouye, M.3
  • 6
    • 0029561894 scopus 로고
    • Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain
    • Denzer, A.J., C.E. Nabholz, and M. Spiess. 1995. Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain. EMBO (Eur. Mol. Biol. Organ.) J. 14:6311-6317.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 6311-6317
    • Denzer, A.J.1    Nabholz, C.E.2    Spiess, M.3
  • 7
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis, L., E. Clauser, D.O. Morgan, M. Edery, R.A. Roth, and W.J. Rutter. 1986. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell. 45:721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.A.5    Rutter, W.J.6
  • 8
    • 0031818513 scopus 로고    scopus 로고
    • The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane
    • Eusebio, A., T. Friedberg, and M. Spiess. 1998. The role of the hydrophobic domain in orienting natural signal sequences within the ER membrane. Exp. Cell Res. 241:181-185.
    • (1998) Exp. Cell Res. , vol.241 , pp. 181-185
    • Eusebio, A.1    Friedberg, T.2    Spiess, M.3
  • 9
    • 0019815069 scopus 로고
    • Cell-surface expression of influenza haemagglutinin from a cloned DNA copy of the RNA gene
    • Gething, M.J., and J. Sambrook. 1981. Cell-surface expression of influenza haemagglutinin from a cloned DNA copy of the RNA gene. Nature: 293: 620-625.
    • (1981) Nature , vol.293 , pp. 620-625
    • Gething, M.J.1    Sambrook, J.2
  • 10
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R., and G. Blobel. 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
  • 11
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich, D., and T.A. Rapoport. 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
  • 12
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gravelin, G., M. Sakaguchi, H. Andersson, and G. von Heijne. 1997. Topological rules for membrane protein assembly in eukaryotic cells. J. Biol. Chem. 272:6119-6127.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6119-6127
    • Gravelin, G.1    Sakaguchi, M.2    Andersson, H.3    Von Heijne, G.4
  • 13
    • 0017157923 scopus 로고
    • Pre-proparathyroid hormone. Evidence for an early biosynthetic precursor of proparathyroid hormone
    • Habener, J.F., J.T. Potts. Jr., and A. Rich. 1976. Pre-proparathyroid hormone. Evidence for an early biosynthetic precursor of proparathyroid hormone. J. Biol. Chem. 251:3893-3899.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3893-3899
    • Habener, J.F.1    Potts J.T., Jr.2    Rich, A.3
  • 14
    • 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.. J.-C. Chen, E.E. Johnson, and A.E. Johnson. 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
  • 16
    • 0032544582 scopus 로고    scopus 로고
    • Transmembrane protein insertion orientation in yeast depends on the charge difference across transmembrane segments, their total hydrophobicity, and its distribution
    • Harley, C.A., J.A. Holt, R. Turner, and D.J. Tipper. 1998. Transmembrane protein insertion orientation in yeast depends on the charge difference across transmembrane segments, their total hydrophobicity, and its distribution. J. Biol. Chem. 273:24963-24971.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24963-24971
    • Harley, C.A.1    Holt, J.A.2    Turner, R.3    Tipper, D.J.4
  • 17
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane spanning proteins
    • Hartmann, E., T.A. Rapoport, and H.F. Lodish. 1989. Predicting the orientation of eukaryotic membrane spanning proteins. Proc. Natl. Acad. Sci. USA. 86:5786-5790.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 18
    • 0032489505 scopus 로고    scopus 로고
    • TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum
    • Hegde, R.S., S. Voigt, T.A. Rapoport, and V.R. Lingappa. 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
  • 19
    • 0030878575 scopus 로고    scopus 로고
    • Membrane protein biosynthesis-all sewn up?
    • High, S., and V. Laird. 1997. Membrane protein biosynthesis-all sewn up? Trends Cell Biol. 7:206-209.
    • (1997) Trends Cell Biol. , vol.7 , pp. 206-209
    • High, S.1    Laird, V.2
  • 20
    • 0028243532 scopus 로고
    • Ubiquitin-assisted dissection of protein transport across membranes
    • Johnsson, N., and A. Varshavsky. 1994. Ubiquitin-assisted dissection of protein transport across membranes. EMBO (Eur. Mol. Biol. Organ.) J. 13:2686-2698.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2686-2698
    • Johnsson, N.1    Varshavsky, A.2
  • 22
    • 0028871658 scopus 로고
    • Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes
    • Leitinger. B., A. Hille-Rehfeld, and M. Spiess. 1995. Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes. Proc. Natl. Acad. Sci. USA. 92:10109-10113.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10109-10113
    • Leitinger, B.1    Hille-Rehfeld, A.2    Spiess, M.3
  • 23
    • 0024454463 scopus 로고
    • Structural requirements for membrane assembly of proteins spanning the membrane several times
    • Lipp, J., N. Flint, M.T. Haeuptle, and B. Dobberstein. 1989. Structural requirements for membrane assembly of proteins spanning the membrane several times. J. Cell Biol. 109:2013-2022.
    • (1989) J. Cell Biol. , vol.109 , pp. 2013-2022
    • Lipp, J.1    Flint, N.2    Haeuptle, M.T.3    Dobberstein, B.4
  • 24
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., M.W. Hofmann, J. Brunner, and B. Dobberstein. 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
  • 25
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-α factor across the ER membrane
    • Matlack, K.E.S., B. Misselwitz, K. Plath, and T.A. Rapoport. 1999. BiP acts as a molecular ratchet during posttranslational transport of prepro-α factor across the ER membrane. Cell. 97:553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.S.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 26
    • 0018073904 scopus 로고
    • Synthesis of preprolactin and conversion to prolactin in intact cells and a cell-free system
    • Maurer, R.A., and D.J. McKean. 1978. Synthesis of preprolactin and conversion to prolactin in intact cells and a cell-free system. J. Biol. Chem. 253: 6315-6318.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6315-6318
    • Maurer, R.A.1    McKean, D.J.2
  • 28
    • 0032572529 scopus 로고    scopus 로고
    • Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane
    • Mothes, W., B. Jungnickel, J. Brunner, and T.A. Rapoport. 1998. Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane. J. Cell Biol. 142:355-364.
    • (1998) J. Cell Biol. , vol.142 , pp. 355-364
    • Mothes, W.1    Jungnickel, B.2    Brunner, J.3    Rapoport, T.A.4
  • 29
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng, D.T., J.D. Brown, and P. Walter. 1996. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134:269-278.
    • (1996) J. Cell Biol. , vol.134 , pp. 269-278
    • Ng, D.T.1    Brown, J.D.2    Walter, P.3
  • 30
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec-proteins and Kar2p
    • Panzner, S., L. Dreier, E. Hartmann, S. Kostka, and T.A. Rapoport. 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
  • 31
    • 0025970881 scopus 로고
    • Topology of eukaryotic type-II memhrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain
    • Parks,. G.D., and R.A. Lamb. 1991. Topology of eukaryotic type-II memhrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain. Cell. 64:777-787.
    • (1991) Cell , vol.64 , pp. 777-787
    • Parks, G.D.1    Lamb, A.R.A.2
  • 32
    • 0031770876 scopus 로고    scopus 로고
    • Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane
    • Pilon, M., K. Romisch, D. Quach, and R. Schekman, 1998. Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane. Mol. Biol. Cell. 9:3455-3473.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3455-3473
    • Pilon, M.1    Romisch, K.2    Quach, D.3    Schekman, R.4
  • 33
    • 0032520083 scopus 로고    scopus 로고
    • Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle
    • Rothe. C., and L. Lehle. 1998. Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle. Eur. J Biochem. 252:16-24.
    • (1998) Eur. J Biochem. , vol.252 , pp. 16-24
    • Rothe, C.1    Lehle, L.2
  • 34
    • 0017753965 scopus 로고
    • Synchronised transmembrane insertion and glycosylation of a nascent memhrane protein
    • Rothman, J.E., and H.F. Lodish. 1977. Synchronised transmembrane insertion and glycosylation of a nascent memhrane protein. Nature. 269:775-780.
    • (1977) Nature , vol.269 , pp. 775-780
    • Rothman, J.E.1    Lodish, H.F.2
  • 35
    • 0026501551 scopus 로고
    • Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge
    • Sakaguchi, M., R. Tomiyoshi, T. Kuroiwa, K. Mihara, and T. Omura, 1992. Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge. Proc. Natl. Acad. Sci. USA. 89:16-19.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 16-19
    • Sakaguchi, M.1    Tomiyoshi, R.2    Kuroiwa, T.3    Mihara, K.4    Omura, T.5
  • 36
    • 0032566739 scopus 로고    scopus 로고
    • Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein
    • Sato, M., R. Hresko, and M. Mueckler. 1998. Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein. J. Biol. Chem. 273:25203-25208.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25203-25208
    • Sato, M.1    Hresko, R.2    Mueckler, M.3
  • 37
    • 0029916898 scopus 로고    scopus 로고
    • The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J
    • Shakin-Eshleman, S.H., S.L. Spitalnik, and L. Kasturi. 1996. The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. J. Biol. Chem. 271:6363-6366.
    • (1996) Biol. Chem. , vol.271 , pp. 6363-6366
    • Shakin-Eshleman, S.H.1    Spitalnik, S.L.2    Kasturi, L.3
  • 38
    • 0029149453 scopus 로고
    • Head or tails - What determines the orientation of proteins in the membrane
    • Spiess, M. 1995. Head or tails - what determines the orientation of proteins in the membrane. FEBS Lett. 369:76-79.
    • (1995) FEBS Lett. , vol.369 , pp. 76-79
    • Spiess, M.1
  • 39
    • 0021922288 scopus 로고
    • Sequence of human asialoglycoprotein receptor cDNA. An internal signal sequence for membrane insertion
    • Spiess, M., A.L. Schwarte, and H.F. Lodish. 1985. Sequence of human asialoglycoprotein receptor cDNA. An internal signal sequence for membrane insertion. J. Biol. Chem. 260:1979-1982.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1979-1982
    • Spiess, M.1    Schwarte, A.L.2    Lodish, H.F.3
  • 40
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • Suzuki, T., H. Park, K. Kitajima, and W.J. Lennarz. 1998. Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J. Biol. Chem. 273:21526-21530.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 41
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum memhrane
    • Voigt, S., B. Jungnickel, E. Hartmann, and T.A. Rapoport. 1996. Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum memhrane. 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
  • 42
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne, G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature. 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • Von Heijne G1
  • 43
    • 0030919649 scopus 로고    scopus 로고
    • Multiple determinants direct the orientation of signal-anchor proteins: The topogenic role of the hydrophobic signal domain
    • Wahlberg, J.M., and M. Spiess. 1997. Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. J. Cell Biol. 137:555-562.
    • (1997) J. Cell Biol. , vol.137 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 44
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and A.E. Johnson. 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
  • 45
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein requires only one signal sequence
    • Wessels, H.P., and M. Spiess. 1988. Insertion of a multispanning membrane protein requires only one signal sequence. Cell. 55:61-70.
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.P.1    Spiess, M.2
  • 46
    • 0025983854 scopus 로고
    • Analysis of protein topology in the endoplasmic reticulum
    • Wessels, H.P., J.P. Beltzer, and M. Spiess. 1991. Analysis of protein topology in the endoplasmic reticulum. Methods Cell Biol. 34:287-302.
    • (1991) Methods Cell Biol. , vol.34 , pp. 287-302
    • Wessels, H.P.1    Beltzer, J.P.2    Spiess, M.3
  • 47
    • 0031923127 scopus 로고    scopus 로고
    • The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum
    • Zimmermann, R. 1998. The role of molecular chaperones in protein transport into the mammalian endoplasmic reticulum. Biol. Chem. 379:275-282.
    • (1998) Biol. Chem. , vol.379 , pp. 275-282
    • Zimmermann, R.1


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