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Volumn 45, Issue 4, 2012, Pages 529-540

Orientational Preferences of Neighboring Helices Can Drive ER Insertion of a Marginally Hydrophobic Transmembrane Helix

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84857439394     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2011.12.024     Document Type: Article
Times cited : (50)

References (38)
  • 3
    • 34547650465 scopus 로고    scopus 로고
    • A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization
    • Buck T.M., Wagner J., Grund S., Skach W.R. A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization. Nat. Struct. Mol. Biol. 2007, 14:762-769.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 762-769
    • Buck, T.M.1    Wagner, J.2    Grund, S.3    Skach, W.R.4
  • 4
    • 34249683488 scopus 로고    scopus 로고
    • Membrane protein structure: prediction versus reality
    • Elofsson A., von Heijne G. Membrane protein structure: prediction versus reality. Annu. Rev. Biochem. 2007, 76:125-140.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 125-140
    • Elofsson, A.1    von Heijne, G.2
  • 7
    • 77953517920 scopus 로고    scopus 로고
    • Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon
    • Fujita H., Kida Y., Hagiwara M., Morimoto F., Sakaguchi M. Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon. Mol. Biol. Cell 2010, 21:2045-2056.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2045-2056
    • Fujita, H.1    Kida, Y.2    Hagiwara, M.3    Morimoto, F.4    Sakaguchi, M.5
  • 8
    • 0028175016 scopus 로고
    • Topological " frustration" in multispanning E. coli inner membrane proteins
    • Gafvelin G., von Heijne G. Topological " frustration" in multispanning E. coli inner membrane proteins. Cell 1994, 77:401-412.
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    von Heijne, G.2
  • 9
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gafvelin G., Sakaguchi M., Andersson H., von Heijne G. Topological rules for membrane protein assembly in eukaryotic cells. J. Biol. Chem. 1997, 272:6119-6127.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6119-6127
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    von Heijne, G.4
  • 10
    • 0042313962 scopus 로고    scopus 로고
    • Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
    • Goder V., Spiess M. Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. EMBO J. 2003, 22:3645-3653.
    • (2003) EMBO J. , vol.22 , pp. 3645-3653
    • Goder, V.1    Spiess, M.2
  • 11
    • 18344400724 scopus 로고    scopus 로고
    • Membrane insertion scanning of the human ileal sodium/bile acid co-transporter
    • Hallén S., Brändén M., Dawson P.A., Sachs G. Membrane insertion scanning of the human ileal sodium/bile acid co-transporter. Biochemistry 1999, 38:11379-11388.
    • (1999) Biochemistry , vol.38 , pp. 11379-11388
    • Hallén, S.1    Brändén, M.2    Dawson, P.A.3    Sachs, G.4
  • 13
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • Heijne G. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 1986, 5:3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Heijne, G.1
  • 16
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M., Junne T., Spiess M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 2004, 43:12716-12722.
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 17
    • 80054991427 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT
    • Hu N.J., Iwata S., Cameron A.D., Drew D. Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 2011, 478:408-411.
    • (2011) Nature , vol.478 , pp. 408-411
    • Hu, N.J.1    Iwata, S.2    Cameron, A.D.3    Drew, D.4
  • 18
    • 78649770531 scopus 로고    scopus 로고
    • Why are polar residues within the membrane core evolutionary conserved?
    • Illergård K., Kauko A., Elofsson A. Why are polar residues within the membrane core evolutionary conserved?. Proteins 2011, 79:79-91.
    • (2011) Proteins , vol.79 , pp. 79-91
    • Illergård, K.1    Kauko, A.2    Elofsson, A.3
  • 19
    • 0029610991 scopus 로고
    • Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase
    • Imperiali B., Hendrickson T.L. Asparagine-linked glycosylation: specificity and function of oligosaccharyl transferase. Bioorg. Med. Chem. 1995, 3:1565-1578.
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 1565-1578
    • Imperiali, B.1    Hendrickson, T.L.2
  • 20
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson M., Nilsson I., von Heijne G. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. 1993, 239:251-256.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    von Heijne, G.3
  • 22
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 23
    • 41949125627 scopus 로고    scopus 로고
    • Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum
    • Lerch-Bader M., Lundin C., Kim H., Nilsson I., von Heijne G. Contribution of positively charged flanking residues to the insertion of transmembrane helices into the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 2008, 105:4127-4132.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4127-4132
    • Lerch-Bader, M.1    Lundin, C.2    Kim, H.3    Nilsson, I.4    von Heijne, G.5
  • 24
    • 57349168025 scopus 로고    scopus 로고
    • Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices
    • Lundin C., Kim H., Nilsson I., White S.H., von Heijne G. Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for N(in)-C(out) and N(out)-C(in) transmembrane helices. Proc. Natl. Acad. Sci. USA 2008, 105:15702-15707.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15702-15707
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.H.4    von Heijne, G.5
  • 25
    • 33750498869 scopus 로고    scopus 로고
    • Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
    • Meindl-Beinker N.M., Lundin C., Nilsson I., White S.H., von Heijne G. Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly. EMBO Rep. 2006, 7:1111-1116.
    • (2006) EMBO Rep. , vol.7 , pp. 1111-1116
    • Meindl-Beinker, N.M.1    Lundin, C.2    Nilsson, I.3    White, S.H.4    von Heijne, G.5
  • 26
    • 0001207024 scopus 로고    scopus 로고
    • N-tail translocation in a eukaryotic polytopic membrane protein: synergy between neighboring transmembrane segments
    • Monné M., Gafvelin G., Nilsson R., von Heijne G. N-tail translocation in a eukaryotic polytopic membrane protein: synergy between neighboring transmembrane segments. Eur. J. Biochem. 1999, 263:264-269.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 264-269
    • Monné, M.1    Gafvelin, G.2    Nilsson, R.3    von Heijne, G.4
  • 27
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson I.M., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 1993, 268:5798-5801.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    von Heijne, G.2
  • 28
    • 0032185234 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins
    • Ota K., Sakaguchi M., von Heijne G., Hamasaki N., Mihara K. Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins. Mol. Cell 1998, 2:495-503.
    • (1998) Mol. Cell , vol.2 , pp. 495-503
    • Ota, K.1    Sakaguchi, M.2    von Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 29
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3
    • Popov M., Tam L.Y., Li J., Reithmeier R.A.F. Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3. J. Biol. Chem. 1997, 272:18325-18332.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.F.4
  • 30
    • 0017753965 scopus 로고
    • Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
    • Rothman J.E., Lodish H.F. Synchronised transmembrane insertion and glycosylation of a nascent membrane protein. Nature 1977, 269:775-780.
    • (1977) Nature , vol.269 , pp. 775-780
    • Rothman, J.E.1    Lodish, H.F.2
  • 31
    • 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., Tomiyoshi R., Kuroiwa T., Mihara K., Omura T. 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 1992, 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
  • 33
    • 66849131417 scopus 로고    scopus 로고
    • Cellular mechanisms of membrane protein folding
    • Skach W.R. Cellular mechanisms of membrane protein folding. Nat. Struct. Mol. Biol. 2009, 16:606-612.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 606-612
    • Skach, W.R.1
  • 34
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • von Heijne G. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 1989, 341:456-458.
    • (1989) Nature , vol.341 , pp. 456-458
    • von Heijne, G.1
  • 35
    • 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., Spiess M. Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. J. Cell Biol. 1997, 137:555-562.
    • (1997) J. Cell Biol. , vol.137 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 36
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • White S.H., von Heijne G. How translocons select transmembrane helices. Annu Rev Biophys 2008, 37:23-42.
    • (2008) Annu Rev Biophys , vol.37 , pp. 23-42
    • White, S.H.1    von Heijne, G.2
  • 37
    • 4444299420 scopus 로고    scopus 로고
    • Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2)
    • Zhang E.Y., Phelps M.A., Banerjee A., Khantwal C.M., Chang C., Helsper F., Swaan P.W. Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2). Biochemistry 2004, 43:11380-11392.
    • (2004) Biochemistry , vol.43 , pp. 11380-11392
    • Zhang, E.Y.1    Phelps, M.A.2    Banerjee, A.3    Khantwal, C.M.4    Chang, C.5    Helsper, F.6    Swaan, P.W.7
  • 38
    • 34347249218 scopus 로고    scopus 로고
    • Contribution of hydrophobic and electrostatic interactions to the membrane integration of the Shaker K+ channel voltage sensor domain
    • Zhang L., Sato Y., Hessa T., von Heijne G., Lee J.K., Kodama I., Sakaguchi M., Uozumi N. Contribution of hydrophobic and electrostatic interactions to the membrane integration of the Shaker K+ channel voltage sensor domain. Proc. Natl. Acad. Sci. USA 2007, 104:8263-8268.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8263-8268
    • Zhang, L.1    Sato, Y.2    Hessa, T.3    von Heijne, G.4    Lee, J.K.5    Kodama, I.6    Sakaguchi, M.7    Uozumi, N.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.