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Volumn 288, Issue 28, 2013, Pages 20326-20333

Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RESIDUES; ATP-ASE ACTIVITY; BALL AND SOCKETS; CONFORMATIONAL CHANGE; NUCLEOTIDE-BINDING DOMAIN; TRANSMEMBRANE DOMAIN; TRANSMISSION INTERFACES; TRANSPORT MECHANISM;

EID: 84880054199     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.484550     Document Type: Article
Times cited : (39)

References (42)
  • 2
    • 33646078329 scopus 로고    scopus 로고
    • ABC A-subfamily transporters: Structure, function, and disease
    • Kaminski, W. E., Piehler, A., and Wenzel, J. J. (2006) ABC A-subfamily transporters: structure, function, and disease. Biochim. Biophys. Acta 1762, 510-524
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 510-524
    • Kaminski, W.E.1    Piehler, A.2    Wenzel, J.J.3
  • 4
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano, R. L., and Ling, V. (1976) A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta 455, 152-162
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 6
    • 67650685020 scopus 로고    scopus 로고
    • ABC efflux pump-based resistance to chemotherapy drugs
    • Eckford, P. D., and Sharom, F. J. (2009) ABC efflux pump-based resistance to chemotherapy drugs. Chem. Rev. 109, 2989-3011
    • (2009) Chem. Rev. , vol.109 , pp. 2989-3011
    • Eckford, P.D.1    Sharom, F.J.2
  • 7
    • 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 Roninson, I. B. (1986) Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrugresistant human cells. Cell 47, 381-389 (Pubitemid 17210152)
    • (1986) Cell , vol.47 , Issue.3 , pp. 381-389
    • Chen, C.-J.1    Chin, J.E.2    Ueda, K.3
  • 10
    • 12144262818 scopus 로고    scopus 로고
    • Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site
    • DOI 10.1021/bi0485326
    • Lugo, M. R., and Sharom, F. J. (2005) Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site. Biochemistry 44, 643-655 (Pubitemid 40105495)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 643-655
    • Lugo, M.R.1    Sharom, F.J.2
  • 11
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug-translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2009) Identification of residues in the drug-translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis. J. Biol. Chem. 284, 24074-24087
    • (2009) J. Biol. Chem. , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 12
    • 0029121417 scopus 로고
    • Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity
    • Loo, T. W., and Clarke, D. M. (1995) Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity. J. Biol. Chem. 270, 22957-22961
    • (1995) J. Biol. Chem. , vol.270 , pp. 22957-22961
    • Loo, T.W.1    Clarke, D.M.2
  • 13
    • 36849067873 scopus 로고    scopus 로고
    • Catalytic cycle of ATP hydrolysis by P-glycoprotein: Evidence for formation of the E.S reaction intermediate with ATP-γ-S, a nonhydrolyzable analogue of ATP
    • DOI 10.1021/bi701385t
    • Sauna, Z. E., Kim, I. W., Nandigama, K., Kopp, S., Chiba, P., and Ambudkar, S. V. (2007) Catalytic cycle of ATP hydrolysis by P-glycoprotein: evidence for formation of the E.S reaction intermediate with ATPγS, a nonhydrolyzable analogue of ATP. Biochemistry 46, 13787-13799 (Pubitemid 350223906)
    • (2007) Biochemistry , vol.46 , Issue.48 , pp. 13787-13799
    • Sauna, Z.E.1    Kim, I.-W.2    Nandigama, K.3    Kopp, S.4    Chiba, P.5    Ambudkar, S.V.6
  • 14
    • 27144547163 scopus 로고    scopus 로고
    • Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy
    • DOI 10.1021/bi0512445
    • Delannoy, S., Urbatsch, I. L., Tombline, G., Senior, A. E., and Vogel, P. D. (2005) Nucleotide binding to the multidrug resistance P-glycoprotein as studied by ESR spectroscopy. Biochemistry 44, 14010-14019 (Pubitemid 41507481)
    • (2005) Biochemistry , vol.44 , Issue.42 , pp. 14010-14019
    • Delannoy, S.1    Urbatsch, I.L.2    Tombline, G.3    Senior, A.E.4    Vogel, P.D.5
  • 15
    • 0029124166 scopus 로고
    • P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site
    • Urbatsch, I. L., Sankaran, B., Weber, J., and Senior, A. E. (1995) P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic site. J. Biol. Chem. 270, 19383-19390
    • (1995) J. Biol. Chem. , vol.270 , pp. 19383-19390
    • Urbatsch, I.L.1    Sankaran, B.2    Weber, J.3    Senior, A.E.4
  • 16
    • 73649111071 scopus 로고    scopus 로고
    • Understanding polyspecificity of multidrug ABC transporters: Closing in on the gaps in ABCB1
    • Gutmann, D. A., Ward, A., Urbatsch, I. L., Chang, G., and van Veen, H. W. (2010) Understanding polyspecificity of multidrug ABC transporters: closing in on the gaps in ABCB1. Trends Biochem. Sci. 35, 36-42
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 36-42
    • Gutmann, D.A.1    Ward, A.2    Urbatsch, I.L.3    Chang, G.4    Van Veen, H.W.5
  • 17
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • Jin, M. S., Oldham, M. L., Zhang, Q., and Chen, J. (2012) Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490, 566-569
    • (2012) Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.3    Chen, J.4
  • 18
    • 2442597224 scopus 로고    scopus 로고
    • 939 in Transmembrane Segment 11 of Human P-glycoprotein
    • DOI 10.1074/jbc.M400229200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2004) Val-133 and Cys-137 in transmembrane segment 2 are close to residues Arg-935 and Gly-939 in transmembrane segment 11 of human P-glycoprotein. J. Biol. Chem. 279, 18232-18238 (Pubitemid 38623236)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18232-18238
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 19
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • DOI 10.1042/BJ20060012
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2006) Transmembrane segment 1 of human P-glycoprotein contributes to the drug binding pocket. Biochem. J. 396, 537-545 (Pubitemid 44228168)
    • (2006) Biochemical Journal , vol.396 , Issue.3 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 20
    • 36148958644 scopus 로고    scopus 로고
    • Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites
    • DOI 10.1074/jbc.M706175200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2007) Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites. J. Biol. Chem. 282, 32043-32052 (Pubitemid 350106425)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 32043-32052
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 21
    • 54049113919 scopus 로고    scopus 로고
    • Arginines in the first transmembrane segment promote maturation of a P-glycoprotein processing mutant by hydrogen bond interactions with tyrosines in transmembrane segment 11
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2008) Arginines in the first transmembrane segment promote maturation of a P-glycoprotein processing mutant by hydrogen bond interactions with tyrosines in transmembrane segment 11. J. Biol. Chem. 283, 24860-24870
    • (2008) J. Biol. Chem. , vol.283 , pp. 24860-24870
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 22
    • 84877763551 scopus 로고    scopus 로고
    • A salt bridge in intracellular loop 2 is essential for folding of human P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (2013) A salt bridge in intracellular loop 2 is essential for folding of human P-glycoprotein. Biochemistry 52, 3194-3196
    • (2013) Biochemistry , vol.52 , pp. 3194-3196
    • Loo, T.W.1    Clarke, D.M.2
  • 23
    • 38549085409 scopus 로고    scopus 로고
    • Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5)
    • Ravna, A. W., Sylte, I., and Sager, G. (2007) Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5). Theor. Biol. Med. Model. 4, 33
    • (2007) Theor. Biol. Med. Model. , vol.4 , pp. 33
    • Ravna, A.W.1    Sylte, I.2    Sager, G.3
  • 24
    • 47049126229 scopus 로고    scopus 로고
    • Identification of putative binding sites of P-glycoprotein based on its homology model
    • Globisch, C., Pajeva, I. K., and Wiese, M. (2008) Identification of putative binding sites of P-glycoprotein based on its homology model. ChemMed-Chem 3, 280-295
    • (2008) ChemMed-Chem , vol.3 , pp. 280-295
    • Globisch, C.1    Pajeva, I.K.2    Wiese, M.3
  • 25
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • DOI 10.1038/nature05155, PII NATURE05155
    • Dawson, R. J., and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (Pubitemid 44387602)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 26
    • 0028245416 scopus 로고
    • Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (1994) Functional consequences of glycine mutations in the predicted cytoplasmic loops of P-glycoprotein. J. Biol. Chem. 269, 7243-7248 (Pubitemid 24217914)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7243-7248
    • Loo, T.W.1    Clarke, D.M.2
  • 28
    • 33847122608 scopus 로고    scopus 로고
    • Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones
    • DOI 10.1124/mol.106.029926
    • Wang, Y., Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2007) Modulating the folding of P-glycoprotein and cystic fibrosis transmembrane conductance regulator truncation mutants with pharmacological chaperones. Mol. Pharmacol. 71, 751-758 (Pubitemid 46294086)
    • (2007) Molecular Pharmacology , vol.71 , Issue.3 , pp. 751-758
    • Wang, Y.1    Loo, T.W.2    Bartlett, M.C.3    Clarke, D.M.4
  • 29
    • 0029100095 scopus 로고
    • Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities
    • Loo, T. W., and Clarke, D. M. (1995) Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities. J. Biol. Chem. 270, 21449-21452
    • (1995) J. Biol. Chem. , vol.270 , pp. 21449-21452
    • Loo, T.W.1    Clarke, D.M.2
  • 30
    • 84864535297 scopus 로고    scopus 로고
    • The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely together
    • Loo, T. W., Bartlett, M. C., Detty, M. R., and Clarke, D. M. (2012) The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely together. J. Biol. Chem. 287, 26806-26816
    • (2012) J. Biol. Chem. , vol.287 , pp. 26806-26816
    • Loo, T.W.1    Bartlett, M.C.2    Detty, M.R.3    Clarke, D.M.4
  • 31
    • 0033609856 scopus 로고    scopus 로고
    • The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface
    • Loo, T. W., and Clarke, D. M. (1999) The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface. J. Biol. Chem. 274, 24759-24765
    • (1999) J. Biol. Chem. , vol.274 , pp. 24759-24765
    • Loo, T.W.1    Clarke, D.M.2
  • 32
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators
    • DOI 10.1074/jbc.272.2.709
    • Loo, T. W., and Clarke, D. M. (1997) Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators. J. Biol. Chem. 272, 709-712 (Pubitemid 27034553)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 33
    • 0037687304 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: Direct evidence for the substrate-induced fit mechanism for drug binding
    • DOI 10.1074/jbc.C300073200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Substrate-induced conformational changes in the transmembrane segments of human P-glycoprotein: direct evidence for the substrate-induced fit mechanism for drug binding. J. Biol. Chem. 278, 13603-13606 (Pubitemid 36799891)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13603-13606
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 35
    • 0037160075 scopus 로고    scopus 로고
    • A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein
    • DOI 10.1074/jbc.M206479200
    • Omote, H., and Al-Shawi, M. K. (2002) A novel electron paramagnetic resonance approach to determine the mechanism of drug transport by P-glycoprotein. J. Biol. Chem. 277, 45688-45694 (Pubitemid 36159181)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45688-45694
    • Omote, H.1    Al-Shawi, M.K.2
  • 36
    • 0347379911 scopus 로고    scopus 로고
    • Methanethiosulfonate Derivatives of Rhodamine and Verapamil Activate Human P-glycoprotein at Different Sites
    • DOI 10.1074/jbc.M310448200
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2003) Methanethiosulfonate derivatives of rhodamine and verapamil activate human P-glycoprotein at different sites. J. Biol. Chem. 278, 50136-50141 (Pubitemid 37548851)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50136-50141
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 38
  • 39
    • 84862890003 scopus 로고    scopus 로고
    • Catalytic transitions in the human MDR1 P-glycoprotein drug binding sites
    • Wise, J. G. (2012) Catalytic transitions in the human MDR1 P-glycoprotein drug binding sites. Biochemistry 51, 5125-5141
    • (2012) Biochemistry , vol.51 , pp. 5125-5141
    • Wise, J.G.1
  • 40
    • 0030775639 scopus 로고    scopus 로고
    • Disease-associated mutations in cytoplasmic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel
    • DOI 10.1021/bi9712652
    • Seibert, F. S., Jia, Y., Mathews, C. J., Hanrahan, J. W., Riordan, J. R., Loo, T. W., and Clarke, D. M. (1997) Disease-associated mutations in cytoplasmic loops 1 and 2 of cystic fibrosis transmembrane conductance regulator impede processing or opening of the channel. Biochemistry 36, 11966-11974 (Pubitemid 27424126)
    • (1997) Biochemistry , vol.36 , Issue.39 , pp. 11966-11974
    • Seibert, F.S.1    Jia, Y.2    Mathews, C.J.3    Hanrahan, J.W.4    Riordan, J.R.5    Loo, T.W.6    Clarke, D.M.7
  • 41
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare, D., Oldham, M. L., Orelle, C., Davidson, A. L., and Chen, J. (2009) Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 33, 528-536
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 42
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • DOI 10.1093/emboj/16.11.3066
    • Mourez, M., Hofnung, M., and Dassa, E. (1997) Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16, 3066-3077 (Pubitemid 27234946)
    • (1997) EMBO Journal , vol.16 , Issue.11 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3


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