메뉴 건너뛰기




Volumn 2, Issue 4, 1998, Pages 495-503

Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROCYTE BAND 3 PROTEIN; MEMBRANE PROTEIN; MESSENGER RNA;

EID: 0032185234     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(00)80149-5     Document Type: Article
Times cited : (94)

References (42)
  • 1
    • 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
  • 2
    • 0030064680 scopus 로고    scopus 로고
    • A two-step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin, D., Bost, S., Vassalli, J.-D., and Strub, K. (1996). A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15, 468-478.
    • (1996) EMBO J. , vol.15 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, J.-D.3    Strub, K.4
  • 3
    • 0032006712 scopus 로고    scopus 로고
    • The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins
    • Bibi, E. (1998). The role of the ribosome-translocon complex in translation and assembly of polytopic membrane proteins. Trends Biochem. Sci. 23, 51-55.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 51-55
    • Bibi, E.1
  • 4
    • 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
  • 5
    • 0028568176 scopus 로고
    • TopPred II: An improved software for membrane protein structure predictions
    • Claros, M.G., and von Heijne, G. (1994). TopPred II: an improved software for membrane protein structure predictions. CABIOS 10, 685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, M.G.1    Von Heijne, G.2
  • 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., Nabholz, C.E., and Spiess, M. (1995). Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain. EMBO J. 14, 6311-6317.
    • (1995) EMBO J. , vol.14 , pp. 6311-6317
    • Denzer, A.J.1    Nabholz, C.E.2    Spiess, M.3
  • 7
    • 0027986795 scopus 로고
    • Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II
    • Fukuda, M., Aruga, J., Niinobe, M., Aimoto, S., and Mikoshiba, K. (1994). Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II. J. Biol. Chem. 269, 29206-29211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29206-29211
    • Fukuda, M.1    Aruga, J.2    Niinobe, M.3    Aimoto, S.4    Mikoshiba, K.5
  • 8
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eukaryotic cells
    • Gafvelin, G., Sakaguchi, M., Andersson, H., and 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
  • 9
    • 0030860847 scopus 로고    scopus 로고
    • Proteolytic cleavage sites of band 3 protein in alkali-treated membranes: Fidelity of hydropathy prediction for band 3 protein
    • Hamasaki, N., Okubo, K., Kuma, H., Kang, D., and Yae, Y. (1997). Proteolytic cleavage sites of band 3 protein in alkali-treated membranes: fidelity of hydropathy prediction for band 3 protein. J. Biochem. 722, 577-585.
    • (1997) J. Biochem. , vol.722 , pp. 577-585
    • Hamasaki, N.1    Okubo, K.2    Kuma, H.3    Kang, D.4    Yae, Y.5
  • 10
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeablility 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 permeablility 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
    • 0029924441 scopus 로고    scopus 로고
    • Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol
    • Hegde, R.S., and Lingappa, V.R. (1996). Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol. Cell 85, 217-228.
    • (1996) Cell , vol.85 , pp. 217-228
    • Hegde, R.S.1    Lingappa, V.R.2
  • 13
    • 0030782178 scopus 로고    scopus 로고
    • Membrane protein biogenesis: Regulated complexity at the endoplasmic reticulum
    • Hegde, R.S., and Lingappa, V.R. (1997). Membrane protein biogenesis: regulated complexity at the endoplasmic reticulum. Cell 91, 575-582.
    • (1997) Cell , vol.91 , pp. 575-582
    • Hegde, R.S.1    Lingappa, V.R.2
  • 14
    • 0026909328 scopus 로고
    • Mechanisms that determine the transmembrane disposition of proteins
    • High, S., and Dobberstein, B. (1992). Mechanisms that determine the transmembrane disposition of proteins. Curr. Opin. Cell Biol. 4, 581-586.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 581-586
    • High, S.1    Dobberstein, B.2
  • 15
    • 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, 50-73.
    • (1983) Methods Enzymol. , vol.96 , pp. 50-73
    • Jackson, R.J.1    Hunt, T.2
  • 16
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B., and Rapoport, T.A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 17
    • 0029960038 scopus 로고    scopus 로고
    • Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins
    • Kuroiwa, T., Sakaguchi, M., Omura, T., and Mihara, K. (1996). Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins. J. Biol. Chem. 271, 6423-6428.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6423-6428
    • Kuroiwa, T.1    Sakaguchi, M.2    Omura, T.3    Mihara, K.4
  • 18
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B., and Rapoport, T.A. (1995). Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J. 14, 217-223.
    • (1995) EMBO J. , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 19
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H., and Johnson, A.E. (1997). Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 20
    • 0024316871 scopus 로고
    • Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)
    • Lux, S.E., John, K.M., Kopito, R.R., and Lodish, H.F. (1989). Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1). Proc. Natl. Acad. Sci. USA 86, 9089-9093.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9089-9093
    • Lux, S.E.1    John, K.M.2    Kopito, R.R.3    Lodish, H.F.4
  • 21
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K.E.S., Mothes, W., and Rapoport, T.A. (1998). Protein translocation: tunnel vision. Cell 92, 381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.S.1    Mothes, W.2    Rapoport, T.A.3
  • 23
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosacchryltranferase active site and the endoplasmic reticulum membrane
    • Nilsson, I.M., and von Heijne, G. (1993). Determination of the distance between the oligosacchryltranferase 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
  • 24
    • 0030745799 scopus 로고    scopus 로고
    • Mapping of the ends of transmembrane segments in a polytopic membrane protein
    • Popov, M., Tam, L.Y., Li, J., and Reithmeier, R.A.F. (1997). Mapping of the ends of transmembrane segments in a polytopic membrane protein. J. Biol. Chem. 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
  • 25
    • 0000919524 scopus 로고    scopus 로고
    • Mutational analysis of signal-anchor and stop-transfer sequences in membrane proteins
    • G. von Heijne, ed. (Austin, TX: R. G. Landes Company)
    • Sakaguchi, M. (1997a). Mutational analysis of signal-anchor and stop-transfer sequences in membrane proteins. In Membrane Protein Assembly, G. von Heijne, ed. (Austin, TX: R. G. Landes Company), pp. 135-150.
    • (1997) Membrane Protein Assembly , pp. 135-150
    • Sakaguchi, M.1
  • 26
    • 0013623829 scopus 로고    scopus 로고
    • Topogenic sequences which regulate integration and topology of membrane proteins in the endoplasmic reticulum membrane
    • N. Hamasaki and K. Mihara, eds. (Fukuoka, Japan: Kyushu University Press)
    • Sakaguchi, M. (1997b). Topogenic sequences which regulate integration and topology of membrane proteins in the endoplasmic reticulum membrane. In Membrane Proteins, N. Hamasaki and K. Mihara, eds. (Fukuoka, Japan: Kyushu University Press), pp. 101-116.
    • (1997) Membrane Proteins , pp. 101-116
    • Sakaguchi, M.1
  • 27
    • 0026675770 scopus 로고
    • Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes
    • Sakaguchi, M., Hachiya, N., Mihara, K., and Omura, T. (1992a). 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
  • 28
    • 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., and Omura, T. (1992b). 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
  • 29
    • 0029851127 scopus 로고    scopus 로고
    • Membrane targeting and determination of transmembrane topology of the human vasopressin V2 receptor
    • Schülein, R., Ruta, C., and Rosenthal, W. (1996). Membrane targeting and determination of transmembrane topology of the human vasopressin V2 receptor. J. Biol. Chem. 271, 28844-28852.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28844-28852
    • Schülein, R.1    Ruta, C.2    Rosenthal, W.3
  • 30
    • 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
  • 31
    • 0028343114 scopus 로고
    • Transmembrane orientation and topogenesis of the third and fourth membrane-spanning regions of human P-glycoprotein (MDR1)
    • Skach, W.R., and Lingappa, V.R. (1994). Transmembrane orientation and topogenesis of the third and fourth membrane-spanning regions of human P-glycoprotein (MDR1). Cancer Res. 54, 3202-3209.
    • (1994) Cancer Res. , vol.54 , pp. 3202-3209
    • Skach, W.R.1    Lingappa, V.R.2
  • 32
    • 0028605308 scopus 로고
    • Identification of an internal topogenic signal sequence in human Band 3, the erythrocyte anion exchanger
    • Tam, L.Y., Loo, T.W., Clarke, D.M., and Reithmeier, R.A.F. (1994). Identification of an internal topogenic signal sequence in human Band 3, the erythrocyte anion exchanger. J. Biol. Chem. 269, 32542-32550.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32542-32550
    • Tam, L.Y.1    Loo, T.W.2    Clarke, D.M.3    Reithmeier, R.A.F.4
  • 33
    • 0027410647 scopus 로고
    • Molecular and cellular biology of the erythrocyte anion exchanger (AE1)
    • Tanner, M.J. (1993). Molecular and cellular biology of the erythrocyte anion exchanger (AE1). Semin. Hematol. 30, 34-57.
    • (1993) Semin. Hematol. , vol.30 , pp. 34-57
    • Tanner, M.J.1
  • 34
    • 0031466796 scopus 로고    scopus 로고
    • The structure and function of band 3 (AE1): Recent developments
    • Tanner, M.J.A. (1997). The structure and function of band 3 (AE1): recent developments. Mol. Mem. Biol. 14, 155-165.
    • (1997) Mol. Mem. Biol. , vol.14 , pp. 155-165
    • Tanner, M.J.A.1
  • 35
    • 0024264841 scopus 로고
    • The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence
    • Tanner, M.J., Martin, P.G., and High, S. (1988). The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence. Biochem. J. 256, 703-712.
    • (1988) Biochem. J. , vol.256 , pp. 703-712
    • Tanner, M.J.1    Martin, P.G.2    High, S.3
  • 36
    • 0030919649 scopus 로고    scopus 로고
    • Multiple determinants direct the orientation of signal-anchor proteins: The topogenic role of the hydrophobic signal signal domain
    • Wahlberg, J.M., and Spiess, M. (1997). Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal signal domain. J. Cell Biol. 137, 555-562.
    • (1997) J. Cell Biol. , vol.137 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 37
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for co-translational protein translocation
    • Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for co-translational protein translocation. Methods Enzymol. 96, 84-93.
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 38
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and Johnson, A.E. (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
  • 39
    • 0030888062 scopus 로고    scopus 로고
    • Complementation studies with co-expressed fragments of the human red cell anion transporter (Band 3; AE1)
    • Wang, L., Groves, J.D., Mawby, W.J., and Tanner, M.J.A. (1997). Complementation studies with co-expressed fragments of the human red cell anion transporter (Band 3; AE1). J. Biol. Chem. 272, 10631-10638.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10631-10638
    • Wang, L.1    Groves, J.D.2    Mawby, W.J.3    Tanner, M.J.A.4
  • 40
    • 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., and 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
  • 41
    • 0000119277 scopus 로고
    • The anion exchange proteins: Homology and secondary structure
    • Wood, P.G. (1992). The anion exchange proteins: homology and secondary structure. Prog. Cell Res. 2, 325-352.
    • (1992) Prog. Cell Res. , vol.2 , pp. 325-352
    • Wood, P.G.1
  • 42
    • 0029963423 scopus 로고    scopus 로고
    • Sequence requirements for membrane assembly of polytopic membrane proteins: Molecular dissection of the membrane insertion process and topogenesis of human MDR3 P-glycoprotein
    • Zhang, JT. (1996). Sequence requirements for membrane assembly of polytopic membrane proteins: molecular dissection of the membrane insertion process and topogenesis of human MDR3 P-glycoprotein. Molec. Biol. Cell 7, 1709-1721.
    • (1996) Molec. Biol. Cell , vol.7 , pp. 1709-1721
    • Zhang, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.