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Volumn 54, Issue 12, 1994, Pages 3202-3209

Transmembrane Orientation and Topogenesis of the Third and Fourth Membrane-spanning Regions of Human P-Glycoprotein (MDR1)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; GLYCOPROTEIN P; MESSENGER RNA; PROLACTIN; SIGNAL PEPTIDE;

EID: 0028343114     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (51)

References (54)
  • 1
    • 0019375626 scopus 로고
    • In vitro biogenesis, core glycosylation and membrane integration of opsin
    • Goldman, G., and Blobel, G. In vitro biogenesis, core glycosylation and membrane integration of opsin. J. Cell Biol., 90: 236-242, 1981.
    • (1981) J. Cell Biol. , vol.90 , pp. 236-242
    • Goldman, G.1    Blobel, G.2
  • 2
    • 0020076111 scopus 로고
    • The erythrocyte anion transport protein is cotranslationally inserted into microsomes
    • Braell, W.A., and Lodish, H.F. The erythrocyte anion transport protein is cotranslationally inserted into microsomes. Cell, 28: 23-31, 1982.
    • (1982) Cell , vol.28 , pp. 23-31
    • Braell, W.A.1    Lodish, H.F.2
  • 3
    • 0021251529 scopus 로고
    • Biogenesis of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, an integral glycoprotein of the endoplasmic reticulum
    • Brown, D., and Simoni, R. Biogenesis of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, an integral glycoprotein of the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA, 81: 1674-1678, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1674-1678
    • Brown, D.1    Simoni, R.2
  • 4
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels, H., and Spiess, M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell, 55: 61-70, 1988.
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.1    Spiess, M.2
  • 5
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA, 77: 14961500, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 14961500
    • Blobel, G.1
  • 6
    • 0022827170 scopus 로고
    • Mechanisms of protein translocation across the endoplasmic reticulum membrane
    • Walter, P., and Lingappa, V.R. Mechanisms of protein translocation across the endoplasmic reticulum membrane. Annu. Rev. Cell Biol., 2: 499-516, 1986.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 499-516
    • Walter, P.1    Lingappa, V.R.2
  • 7
    • 0002323314 scopus 로고
    • Intracellular trafficking of pre(pro-) proteins across RER membranes
    • In: Y.P. Loh (ed.), Boca Raton, FL: CRC Press Inc.
    • Skach, W., and Lingappa, V. Intracellular trafficking of pre(pro-) proteins across RER membranes. In: Y.P. Loh (ed.), Mechanisms of Intracellular Trafficking and Processing of Pro-proteins, pp. 19-77. Boca Raton, FL: CRC Press Inc., 1993.
    • (1993) Mechanisms of Intracellular Trafficking and Processing of Pro-proteins , pp. 19-77
    • Skach, W.1    Lingappa, V.2
  • 8
    • 0023729159 scopus 로고
    • Construction of defined polytopic integral transmembrane proteins
    • Rothman, R.E., Andrews, D.W., Calayag, M.C., and Lingappa, V.R. Construction of defined polytopic integral transmembrane proteins. J. Biol. Chem., 263: 10470-10480, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10470-10480
    • Rothman, R.E.1    Andrews, D.W.2    Calayag, M.C.3    Lingappa, V.R.4
  • 9
    • 0024454463 scopus 로고
    • Structural requirements for membrane assembly of proteins spanning the membrane several times
    • Lipp, J., Flint, N., Haeuptle, M.T., and Dobberstein, B. Structural requirements for membrane assembly of proteins spanning the membrane several times. J. Cell Biol., 109: 2013-2022, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 2013-2022
    • Lipp, J.1    Flint, N.2    Haeuptle, M.T.3    Dobberstein, B.4
  • 10
    • 0022358406 scopus 로고
    • Bovine opsin has more than one signal sequence
    • Friedlander, M., and Blobel, G. Bovine opsin has more than one signal sequence. Nature (Lond.), 318: 338-343, 1985.
    • (1985) Nature (Lond.) , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 12
    • 0025745313 scopus 로고
    • The transmembrane topology of the amino terminus of the alpha subunit of the nicotinic acetylcholine receptor
    • Chavez, R.A., and Hall, Z.W. The transmembrane topology of the amino terminus of the alpha subunit of the nicotinic acetylcholine receptor. J. Biol. Chem., 266: 15532-15538, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15532-15538
    • Chavez, R.A.1    Hall, Z.W.2
  • 13
    • 0024329881 scopus 로고
    • The biochemistry of P-glycoprotein-mediated multidrug resistance
    • Endicott, J., and Ling, V. The biochemistry of P-glycoprotein-mediated multidrug resistance. Annu. Rev. Biochem., 58: 137-171, 1989.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 137-171
    • Endicott, J.1    Ling, V.2
  • 14
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M., and Pastan, I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem., 62: 385-427, 1992.
    • (1992) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.1    Pastan, I.2
  • 15
    • 0027548174 scopus 로고
    • P-glycoproteins: mediators of multidrug resistance
    • Germann, U., Pastan, I., and Gottesman, M. P-glycoproteins: mediators of multidrug resistance. Semin. Cell. Biol., 4: 63-76, 1993.
    • (1993) Semin. Cell. Biol. , vol.4 , pp. 63-76
    • Germann, U.1    Pastan, I.2    Gottesman, M.3
  • 17
    • 0024779132 scopus 로고
    • P-glycoprotein: multidrug-resistance and a superfamily of membrane-associated transport proteins
    • Juranka, P.F., Zastawny, R.L., and Ling, V. P-glycoprotein: multidrug-resistance and a superfamily of membrane-associated transport proteins. FASEB, 3: 2583-2592, 1989.
    • (1989) FASEB , vol.3 , pp. 2583-2592
    • Juranka, P.F.1    Zastawny, R.L.2    Ling, V.3
  • 18
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug resistant human cells
    • Chen, C.J., Chin, J.E., Ueda, K., Clark, D.P., Pastan, I., Gottesman, M.M., and Ronninson, I.B. Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug resistant human cells. Cell, 47: 381-389, 1986.
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.J.1    Chin, J.E.2    Ueda, K.3    Clark, D.P.4    Pastan, I.5    Gottesman, M.M.6    Ronninson, I.B.7
  • 19
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros, P., Croop, J., and Housman, D. Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell, 47: 371-380, 1986.
    • (1986) Cell , vol.47 , pp. 371-380
    • Gros, P.1    Croop, J.2    Housman, D.3
  • 21
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • McGrath, J.P., and Varshavsky, A. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature (Lond.), 340: 400-404, 1989.
    • (1989) Nature (Lond.) , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 22
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • Skach, W., Calayag, M.C., and Lingappa, V. Evidence for an alternate model of human P-glycoprotein structure and biogenesis. J. Biol. Chem., 268: 6903-6908, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6903-6908
    • Skach, W.1    Calayag, M.C.2    Lingappa, V.3
  • 23
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycoslyated extracellular loops of mouse P-glycoprotein by in vitro translation
    • Zhang, J.T., and Ling, V. Study of membrane orientation and glycoslyated extracellular loops of mouse P-glycoprotein by in vitro translation. J. Biol. Chem., 266: 18224-18232, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18224-18232
    • Zhang, J.T.1    Ling, V.2
  • 24
    • 0027284115 scopus 로고
    • Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule
    • Zhang, J.T., Duthie, M., and Ling, V. Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule. J. Biol. Chem., 268: 15101-15110, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15101-15110
    • Zhang, J.T.1    Duthie, M.2    Ling, V.3
  • 25
    • 0027519416 scopus 로고
    • Amino terminus assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach, W., and Lingappa, V. Amino terminus assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J. Biol. Chem. 268: 23552-23561, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23552-23561
    • Skach, W.1    Lingappa, V.2
  • 27
    • 0023685557 scopus 로고
    • Sequences beyond cleavage site influence signal peptide function
    • Andrews, D.W., Perara, E., Lesser, C., and Lingappa, V.R. Sequences beyond cleavage site influence signal peptide function. J. Biol. Chem., 263: 15791-15798, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15791-15798
    • Andrews, D.W.1    Perara, E.2    Lesser, C.3    Lingappa, V.R.4
  • 28
    • 0022367193 scopus 로고
    • A former amino terminal signal sequence engineered to an internal location directs translocation of both flanking proteins domains
    • Perara, E., and Lingappa, V.R. A former amino terminal signal sequence engineered to an internal location directs translocation of both flanking proteins domains. J. Cell. Biol., 101: 2292-2301, 1985.
    • (1985) J. Cell. Biol. , vol.101 , pp. 2292-2301
    • Perara, E.1    Lingappa, V.R.2
  • 30
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler, B., Boyd, D., and Beckwith, J. The topological analysis of integral cytoplasmic membrane proteins. J. Membr. Biol., 132: 1-11, 1993.
    • (1993) J. Membr. Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 31
    • 84965825121 scopus 로고    scopus 로고
    • Biogenesis and transmembrane topology of the human CHIP28 water channel in the endoplasmic reticulum
    • in press.
    • Skach W., Shi, L.B., Cayalag, M., Frigeri, A., Lingappa, V., and Verkman, A. Biogenesis and transmembrane topology of the human CHIP28 water channel in the endoplasmic reticulum. J. Cell Biol., in press.
    • J. Cell Biol.
    • Skach, W.1    Shi, L.B.2    Cayalag, M.3    Frigeri, A.4    Lingappa, V.5    Verkman, A.6
  • 32
    • 0023057578 scopus 로고
    • The membrane-spanning segment of invariant chain (I lambda) contains a potentially cleavable signal sequence
    • Lipp, J., and Dobberstein, B. The membrane-spanning segment of invariant chain (I lambda) contains a potentially cleavable signal sequence. Cell, 46: 1103-1112, 1986.
    • (1986) Cell , vol.46 , pp. 1103-1112
    • Lipp, J.1    Dobberstein, B.2
  • 33
    • 0023806486 scopus 로고
    • Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence
    • Schmid, S.R., and Spiess, M. Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence. J. Biol. Chem., 163: 16886-16891, 1988.
    • (1988) J. Biol. Chem. , vol.163 , pp. 16886-16891
    • Schmid, S.R.1    Spiess, M.2
  • 34
    • 0025195720 scopus 로고
    • Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase
    • Nothwehr, S.F., and Gordon, J.I. Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase. J. Biol. Chem., 265: 17202-17208, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17202-17208
    • Nothwehr, S.F.1    Gordon, J.I.2
  • 35
    • 0020381457 scopus 로고
    • Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein
    • Gething, M.J., and Sambrook, J. Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein. Nature (Lond.), 300: 598603, 1982.
    • (1982) Nature (Lond.) , vol.300 , pp. 598603
    • Gething, M.J.1    Sambrook, J.2
  • 36
    • 0020608403 scopus 로고
    • A stop transfer sequence confers predictable transmembrane orientation to a previously secreted protein in cell-free systems
    • Yost, C.S., Hedgpeth, J., and Lingappa, V.R. A stop transfer sequence confers predictable transmembrane orientation to a previously secreted protein in cell-free systems. Cell, 34: 759-766, 1983.
    • (1983) Cell , vol.34 , pp. 759-766
    • Yost, C.S.1    Hedgpeth, J.2    Lingappa, V.R.3
  • 37
    • 0025882870 scopus 로고
    • Systematic analysis of stop-transfer sequence for microsomal membrane
    • Kuroiwa, T., Sakaguchi, M., Mihara, K., and Omura, T. Systematic analysis of stop-transfer sequence for microsomal membrane. J. Biol. Chem., 266: 9251-9255, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9251-9255
    • Kuroiwa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 38
    • 0022006796 scopus 로고
    • Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport
    • Adams, G.A., and Rose, J.K. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell, 41: 1007-1015, 1985.
    • (1985) Cell , vol.41 , pp. 1007-1015
    • Adams, G.A.1    Rose, J.K.2
  • 39
    • 0022358219 scopus 로고
    • Fine structure of a membrane anchor domain
    • Davis, N.G., Boeke, J.D., and Model, P. Fine structure of a membrane anchor domain. J. Mol. Biol., 181: 111-121, 1985.
    • (1985) J. Mol. Biol. , vol.181 , pp. 111-121
    • Davis, N.G.1    Boeke, J.D.2    Model, P.3
  • 41
    • 0025053613 scopus 로고
    • Beta-lactamase as a probe of membrane protein assembly and protein export
    • Broome-Smith, J., Tadayyon, M., and Zhang, Y. Beta-lactamase as a probe of membrane protein assembly and protein export. Mol. Microbiol., 4: 1637-1644, 1990.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1637-1644
    • Broome-Smith, J.1    Tadayyon, M.2    Zhang, Y.3
  • 42
    • 0025330038 scopus 로고
    • lac permiase of Escherichia coli: topology and sequence elements promoting membrane insertion
    • Calamia, J., and Manoil, C. lac permiase of Escherichia coli: topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA, 87: 4937-4941, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4937-4941
    • Calamia, J.1    Manoil, C.2
  • 43
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd, D., Traxler, B., and Beckwith, J. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol., 175: 553-556, 1993.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 44
    • 0026644816 scopus 로고
    • Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins
    • Ooi, C., and Weiss, J. Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins. Cell, 71: 87-96, 1992.
    • (1992) Cell , vol.71 , pp. 87-96
    • Ooi, C.1    Weiss, J.2
  • 45
    • 0026684458 scopus 로고
    • Signal peptides open protein-conducting channels in E
    • Simon, S., and Blobel, G. Signal peptides open protein-conducting channels in E. coli. Cell, 69: 677-684, 1992.
    • (1992) coli. Cell , vol.69 , pp. 677-684
    • Simon, S.1    Blobel, G.2
  • 46
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M., and Blobel, G. A protein-conducting channel in the endoplasmic reticulum. Cell, 65: 371-380, 1991.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 47
    • 0022878780 scopus 로고
    • A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membrane
    • Mize, N.K., Andrews, D.W., and Lingappa, V.R. A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membrane. Cell, 47: 711-719, 1986.
    • (1986) Cell , vol.47 , pp. 711-719
    • Mize, N.K.1    Andrews, D.W.2    Lingappa, V.R.3
  • 49
    • 0025120245 scopus 로고
    • Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein
    • Yost, C.S., Lopez, C.D., Prusiner, S.B., Meyers, R.M., and Lingappa, V.R. Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein. Nature (Lond.), 343: 669-672, 1990.
    • (1990) Nature (Lond.) , vol.343 , pp. 669-672
    • Yost, C.S.1    Lopez, C.D.2    Prusiner, S.B.3    Meyers, R.M.4    Lingappa, V.R.5
  • 50
    • 0025741581 scopus 로고
    • More than just a channel: provocative new features of protein traffic across the ER membrane
    • Lingappa, V.R. More than just a channel: provocative new features of protein traffic across the ER membrane. Cell, 65: 527-530, 1991.
    • (1991) Cell , vol.65 , pp. 527-530
    • Lingappa, V.R.1
  • 51
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoport, T. Transport of proteins across the endoplasmic reticulum membrane. Science (Washington DC), 258: 931-936, 1992.
    • (1992) Science (Washington DC) , vol.258 , pp. 931-936
    • Rapoport, T.1
  • 52
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich, D. and Rapoport, T. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell, 75: 615-630, 1993
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.2
  • 53
    • 0027229977 scopus 로고
    • Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion
    • High, S., Andersen, S., Goerlich, D., Hartmann, E., Prehn, S., Rapoport, T., and Dobberstein, B. Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J. Cell Biol., 121: 743-750, 1993.
    • (1993) J. Cell Biol. , vol.121 , pp. 743-750
    • High, S.1    Andersen, S.2    Goerlich, D.3    Hartmann, E.4    Prehn, S.5    Rapoport, T.6    Dobberstein, B.7
  • 54
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S., Whitfield, K., Vogel, J., Rose, M., and Scheckman, R. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell, 69: 353-365, 1992.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.1    Whitfield, K.2    Vogel, J.3    Rose, M.4    Scheckman, R.5


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