메뉴 건너뛰기




Volumn 159, Issue 1, 1997, Pages 1-20

Membrane topology motifs in the SGLT cotransporter family

Author keywords

Helical hairpin; Hydrophobicity; Membrane insertion; Memsat; Phylogenetic analysis; Predict; Protein

Indexed keywords

GLUCOSE TRANSPORTER;

EID: 0030924414     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900264     Document Type: Review
Times cited : (194)

References (75)
  • 2
    • 0027473683 scopus 로고
    • Sec dependent and sec independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
    • Andersson, H., von Heijne, G. 1993. Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length. EMBO J. 12:683-691
    • (1993) EMBO J. , vol.12 , pp. 683-691
    • Andersson, H.1    Von Heijne, G.2
  • 3
    • 0028291426 scopus 로고
    • Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane
    • Andersson, H., von Heijne, G. 1994. Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane. FEBS Lett. 347:169-172
    • (1994) FEBS Lett. , vol.347 , pp. 169-172
    • Andersson, H.1    Von Heijne, G.2
  • 4
    • 0029790978 scopus 로고    scopus 로고
    • In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force
    • Bassilana, M., Gwizdek, C. 1996. In vivo membrane assembly of the E. coli polytopic protein, melibiose permease, occurs via a Sec-independent process which requires the protonmotive force. EMBO J. 15:5202-5208
    • (1996) EMBO J. , vol.15 , pp. 5202-5208
    • Bassilana, M.1    Gwizdek, C.2
  • 5
    • 0031021424 scopus 로고    scopus 로고
    • -]-coupled gamma-aminobutyric acid transporter from rat brain
    • -]-coupled gamma-aminobutyric acid transporter from rat brain. J. Biol. Chem. 272:1203-1210
    • (1997) J. Biol. Chem. , vol.272 , pp. 1203-1210
    • Bennett, E.R.1    Kanner, B.I.2
  • 7
    • 0027207386 scopus 로고
    • Membrane topology of the glucose transporter of Escherichia coli
    • Buhr, A., Erni, B. 1993. Membrane topology of the glucose transporter of Escherichia coli. J. Biol. Chem. 268:11599-11603
    • (1993) J. Biol. Chem. , vol.268 , pp. 11599-11603
    • Buhr, A.1    Erni, B.2
  • 8
    • 0025330038 scopus 로고
    • lac permease of Escherichia coli: Topology and sequence elements promoting membrane insertion
    • Calamia, J., Manoil, C. 1990. lac permease of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA 87:4937-4941
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2
  • 9
    • 0027942129 scopus 로고
    • Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly
    • Cao, G., Cheng, S., Whitley, P., von Heijne, G., Kuhn, A., Dalbey, R.E. 1994. Synergistic insertion of two hydrophobic regions drives Sec-independent membrane protein assembly. J. Biol. Chem. 269:26898-26903
    • (1994) J. Biol. Chem. , vol.269 , pp. 26898-26903
    • Cao, G.1    Cheng, S.2    Whitley, P.3    Von Heijne, G.4    Kuhn, A.5    Dalbey, R.E.6
  • 10
    • 0029974176 scopus 로고    scopus 로고
    • Antibodies as tools to study the structure of membrane proteins: The case of the nicotinic acetylcholine receptor
    • Conti-Fine, B.M., Lei, S.J., McLane, K.E. 1996. Antibodies as tools to study the structure of membrane proteins: The case of the nicotinic acetylcholine receptor. Annu. Rev. Biophys. Biomol. Struct. 25:197-229
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 197-229
    • Conti-Fine, B.M.1    Lei, S.J.2    McLane, K.E.3
  • 12
    • 0029160967 scopus 로고
    • Directioality in protein translocation across membranes: The N-tail phenomenon
    • Dalbey, R.E., Kuhn, A., von Heijne, G. 1995. Directioality in protein translocation across membranes: the N-tail phenomenon. Trends Cell Biol. 5:380-383
    • (1995) Trends Cell Biol. , vol.5 , pp. 380-383
    • Dalbey, R.E.1    Kuhn, A.2    Von Heijne, G.3
  • 14
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., Schwarz, E., Komaromy, M., Wall, R. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 15
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman, D.M., Steitz, T.A. 1981. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23:411-422
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 17
    • 0029935866 scopus 로고    scopus 로고
    • Progressive alignment of amino acid sequences and construction of phylogenetic trees from them
    • Feng, D.F., Doolittle, R.F. 1996. Progressive alignment of amino acid sequences and construction of phylogenetic trees from them. Methods Enzymol. 266:368-382
    • (1996) Methods Enzymol. , vol.266 , pp. 368-382
    • Feng, D.F.1    Doolittle, R.F.2
  • 18
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gafvelin, G., Sakaguchi, M., Andersson, H., von Heijne, G. 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
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    Von Heijne, G.4
  • 19
    • 0028175016 scopus 로고
    • Topological "frustration" in multispanning. E. coli inner membrane proteins
    • Gafvelin, G., von Heijne, G. 1994. Topological "frustration" in multispanning. E. coli inner membrane proteins. Cell 77:401-412
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    Von Heijne, G.2
  • 21
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., Rapoport, T.A., Lodish, H.F. 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
  • 25
    • 0029947674 scopus 로고    scopus 로고
    • Membrane topology of the mannose transporter of Escherichia coli K12
    • Huber, F., Erni, B. 1996. Membrane topology of the mannose transporter of Escherichia coli K12. Eur. J. Biochem. 239:810-817
    • (1996) Eur. J. Biochem. , vol.239 , pp. 810-817
    • Huber, F.1    Erni, B.2
  • 26
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R.E., White, S.H. 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry 28:3421-3437
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 27
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membarne protein structure and topology
    • Jones, D.T., Taylor, W.R., Thornton, J.M. 1994. A model recognition approach to the prediction of all-helical membarne protein structure and topology. Biochemistry 33:3038-3049
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 29
    • 0028044629 scopus 로고
    • +/glucose cotransporter SGLT2. Delineation of the major renal reabsorptive mechanism for D-glucose
    • +/glucose cotransporter SGLT2. Delineation of the major renal reabsorptive mechanism for D-glucose. J. Clin. Invest. 93:397-404
    • (1994) J. Clin. Invest. , vol.93 , pp. 397-404
    • Kanai, Y.1    Lee, W.S.2    You, G.3    Brown, D.4    Hediger, M.A.5
  • 32
    • 85047694884 scopus 로고
    • Alterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY
    • Kuhn, A. 1988. Alterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY. Eur. J. Biochem. 177:267-271
    • (1988) Eur. J. Biochem. , vol.177 , pp. 267-271
    • Kuhn, A.1
  • 33
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 34
    • 0026516666 scopus 로고
    • Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion
    • Lee, J.I., Kuhn, A., Dalbey, R.E. 1992. Distinct domains of an oligotopic membrane protein are Sec-dependent and Sec-independent for membrane insertion. J. Biol. Chem. 267:938-943
    • (1992) J. Biol. Chem. , vol.267 , pp. 938-943
    • Lee, J.I.1    Kuhn, A.2    Dalbey, R.E.3
  • 36
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T.W., Clarke, D.M. 1995. Membrane topology of a cysteine-less mutant of human P-glycoprotein. J. Biol. Chem. 270:843-848
    • (1995) J. Biol. Chem. , vol.270 , pp. 843-848
    • Loo, T.W.1    Clarke, D.M.2
  • 38
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger, M.D., Saier, M.H. 1993. A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport [see comments]. Trends Biochem. Sci. 18:13-20
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 13-20
    • Marger, M.D.1    Saier, M.H.2
  • 39
    • 0026521552 scopus 로고
    • The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins
    • Nakashima, H., Nishikawa, K. 1992. The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins. FEBS Lett. 303:141-146
    • (1992) FEBS Lett. , vol.303 , pp. 141-146
    • Nakashima, H.1    Nishikawa, K.2
  • 40
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson, I.M., von Heijne, G. 1993. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J. Biol. Chem. 268:5798-5801
    • (1993) J. Biol. Chem. , vol.268 , pp. 5798-5801
    • Nilsson, I.M.1    Von Heijne, G.2
  • 41
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olender, E.H., Simoni, R.D. 1992. The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267:4223-4235
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olender, E.H.1    Simoni, R.D.2
  • 42
    • 0031030990 scopus 로고    scopus 로고
    • Analysis of the transmembrane topology of the glycine transporter GLYT1
    • Olivares, L., Aragon, C., Gimenez, C., Zafra, F. 1997. Analysis of the transmembrane topology of the glycine transporter GLYT1. J. Biol. Chem. 272:1211-1217
    • (1997) J. Biol. Chem. , vol.272 , pp. 1211-1217
    • Olivares, L.1    Aragon, C.2    Gimenez, C.3    Zafra, F.4
  • 47
    • 0027337017 scopus 로고
    • 2-terminal positively charged residues in establishing membrane protein topology
    • 2-terminal positively charged residues in establishing membrane protein topology. J. Biol. Chem. 268:19101-19109
    • (1993) J. Biol. Chem. , vol.268 , pp. 19101-19109
    • Parks, G.D.1    Lamb, R.A.2
  • 48
    • 0026651391 scopus 로고
    • Dynamic programming algorithms for biological sequence comparison
    • Pearson, W.R., Miller, W. 1992. Dynamic programming algorithms for biological sequence comparison. Methods Enzymol. 210:575-601
    • (1992) Methods Enzymol. , vol.210 , pp. 575-601
    • Pearson, W.R.1    Miller, W.2
  • 49
    • 0030020734 scopus 로고    scopus 로고
    • Topology prediction of membrane proteins
    • Persson, B., Argos, P. 1996. Topology prediction of membrane proteins. Protein Science 5:363-371
    • (1996) Protein Science , vol.5 , pp. 363-371
    • Persson, B.1    Argos, P.2
  • 50
    • 0029932862 scopus 로고    scopus 로고
    • Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis
    • Pourcher, T., Bibi, E., Kaback, H.R., Leblanc, G. 1996. Membrane topology of the melibiose permease of Escherichia coli studied by melB-phoA fusion analysis. Biochemistry 35:4161-4168
    • (1996) Biochemistry , vol.35 , pp. 4161-4168
    • Pourcher, T.1    Bibi, E.2    Kaback, H.R.3    Leblanc, G.4
  • 51
    • 0029957853 scopus 로고    scopus 로고
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake. Eur. J. Biochem. 239:732-736
    • (1996) Eur. J. Biochem. , vol.239 , pp. 732-736
    • Quick, M.1    Tebbe, S.2    Jung, H.3
  • 53
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., Sander, C. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 54
    • 0029283519 scopus 로고
    • SecA-dependence of the translocation of a large periplasmic loop in the Escherichia coli MalF inner membrane protein is a function of sequence context
    • Saaf, A., Andersson, H., Gafvelin, G., von Heijne, G. 1995. SecA-dependence of the translocation of a large periplasmic loop in the Escherichia coli MalF inner membrane protein is a function of sequence context. Mol. Membr. Biol. 12:209-215
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 209-215
    • Saaf, A.1    Andersson, H.2    Gafvelin, G.3    Von Heijne, G.4
  • 55
    • 0028345374 scopus 로고
    • Computer-aided analyses of transport protein sequences: Gleaning evidence concerning function, structure, biogenesis, and evolution
    • Saier, M.H. 1994. Computer-aided analyses of transport protein sequences: gleaning evidence concerning function, structure, biogenesis, and evolution. Microbiol. Rev. 58:71-93
    • (1994) Microbiol. Rev. , vol.58 , pp. 71-93
    • Saier, M.H.1
  • 58
    • 0029848950 scopus 로고    scopus 로고
    • Accessibility and environment probing using cysteine residues introduced along the putative transmembrane domain of the major coat protein of bacteriophage M13
    • Spruijt, R.B., Wolfs, C.J., Verver, J.W., Hemminga, M.A. 1996. Accessibility and environment probing using cysteine residues introduced along the putative transmembrane domain of the major coat protein of bacteriophage M13. Biochemistry 35:10383-10391
    • (1996) Biochemistry , vol.35 , pp. 10383-10391
    • Spruijt, R.B.1    Wolfs, C.J.2    Verver, J.W.3    Hemminga, M.A.4
  • 59
    • 0026052185 scopus 로고
    • Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions
    • Sugiyama, J.E., Mahmoodian, S., Jacobson, G.R. 1991. Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions. Proc. Natl. Acad. Sci. USA 88:9603-9607
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9603-9607
    • Sugiyama, J.E.1    Mahmoodian, S.2    Jacobson, G.R.3
  • 60
    • 0025980323 scopus 로고
    • +-dependent active type and erythrocyte/ HepG2-glucose transporters in rat kidney: Immunofluorescence and immunogold study
    • +-dependent active type and erythrocyte/ HepG2-glucose transporters in rat kidney: immunofluorescence and immunogold study. J. Histochem. Cytochem. 39:287-298
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 287-298
    • Takata, K.1    Kasahara, T.2    Kasahara, M.3    Ezaki, O.4    Hirano, H.5
  • 61
    • 0026718498 scopus 로고
    • Dependence of reaction rate of 5,5′-dithiobis-(2-nitrobenzoic acid) to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations
    • Takeda, K., Shigemura, A., Hamada, S., Gu, W., Fang, D., Sasa, K., Hachiya, K. 1992. Dependence of reaction rate of 5,5′-dithiobis-(2-nitrobenzoic acid) to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations. J. Protein Chem. 11:187-192
    • (1992) J. Protein Chem. , vol.11 , pp. 187-192
    • Takeda, K.1    Shigemura, A.2    Hamada, S.3    Gu, W.4    Fang, D.5    Sasa, K.6    Hachiya, K.7
  • 62
    • 0027752961 scopus 로고
    • + transport protein (RhaT) from enterobacteria
    • + transport protein (RhaT) from enterobacteria. J. Biol. Chem. 268:26850-26857
    • (1993) J. Biol. Chem. , vol.268 , pp. 26850-26857
    • Tate, C.G.1    Henderson, P.J.2
  • 63
    • 0027478779 scopus 로고
    • The topological analysis of intergral cytoplasmic membrane proteins
    • Traxler, B., Boyd, D., Beckwith, J. 1993. The topological analysis of intergral cytoplasmic membrane proteins. J. Membrane Biol. 132:1-11.
    • (1993) J. Membrane Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 65
    • 0029665082 scopus 로고    scopus 로고
    • +-dependent glucose cotransporter (SGLT1): Maintenance of surface expression and global transport function with selective perturbation of transport kinetics and polarized expression
    • +-dependent glucose cotransporter (SGLT1): maintenance of surface expression and global transport function with selective perturbation of transport kinetics and polarized expression. J. Biol. Chem. 271:7738-7744
    • (1996) J. Biol. Chem. , vol.271 , pp. 7738-7744
    • Turner, J.R.1    Lencer, W.I.2    Carlson, S.3    Madara, J.L.4
  • 66
    • 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, G.1
  • 67
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 68
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne, G., Gavel, Y. 1988. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:671-678
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 69
    • 0028834958 scopus 로고
    • Properties of N-terminal tails in G-protein coupled receptors: A statistical study
    • Wallin, E., von Heijne, G. 1995. Properties of N-terminal tails in G-protein coupled receptors: a statistical study. Protein Eng. 8:693-698
    • (1995) Protein Eng. , vol.8 , pp. 693-698
    • Wallin, E.1    Von Heijne, G.2
  • 70
    • 0000391729 scopus 로고
    • (White, S.H., ed) Oxford University Press, New York
    • White, S.H. 1994. Membrane Protein Structure (White, S.H., ed) pp. 97-124, Oxford University Press, New York
    • (1994) Membrane Protein Structure , pp. 97-124
    • White, S.H.1
  • 71
    • 0025304452 scopus 로고
    • Observations concerning topology and locations of helix ends of membrane proteins of known structure
    • White, S.H., Jacobs, R.E. 1990. Observations concerning topology and locations of helix ends of membrane proteins of known structure. J. Membrane Biol. 115:145-158
    • (1990) J. Membrane Biol. , vol.115 , pp. 145-158
    • White, S.H.1    Jacobs, R.E.2
  • 72
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson, B.M., Critchley, A.J., Stirling, C.J. 1996. Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271:25590-25597
    • (1996) J. Biol. Chem. , vol.271 , pp. 25590-25597
    • Wilkinson, B.M.1    Critchley, A.J.2    Stirling, C.J.3
  • 74
    • 0027992026 scopus 로고
    • Site-specific alteration of arginine 376, the unique positively charged amino acid residue in the mid-membrane-spanning regions of the proline carrier of Escherichia coli
    • Yamato, I., Kotani, M., Oka, Y., Anraku, Y. 1994. Site-specific alteration of arginine 376, the unique positively charged amino acid residue in the mid-membrane-spanning regions of the proline carrier of Escherichia coli. J. Biol. Chem. 269:5720-5724
    • (1994) J. Biol. Chem. , vol.269 , pp. 5720-5724
    • Yamato, I.1    Kotani, M.2    Oka, Y.3    Anraku, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.