메뉴 건너뛰기




Volumn 399, Issue 2, 2006, Pages 315-323

Conformational and functional characterization of trapped complexes of the P-glycoprotein multidrug transporter

Author keywords

ATP binding cassette superfamily (ABC superfamily); Fluorescence quenching; Multidrug resistance; Nucleotide binding domain; P glycoprotein (Pgp); Transition state

Indexed keywords

ATP-BINDING CASSETTE SUPERFAMILY (ABC SUPERFAMILY); FLUORESCENCE QUENCHING; MULTIDRUG RESISTANCE; NUCLEOTIDE-BINDING DOMAIN; P-GLYCOPROTEIN (PGP); TRANSITION STATE;

EID: 33749994338     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060015     Document Type: Article
Times cited : (34)

References (50)
  • 1
    • 0346814102 scopus 로고    scopus 로고
    • Phylogenetic and functional classification of ABC (ATP-binding cassette) systems
    • (Holland, I. B., Cole, S. P. C., Kuchler, K. and Higgins, C. F., eds.), Academic Press, London
    • Dassa, E. (2003) Phylogenetic and functional classification of ABC (ATP-binding cassette) systems. In ABC Proteins: from Bacteria to Man (Holland, I. B., Cole, S. P. C., Kuchler, K. and Higgins, C. F., eds.), pp. 3-35, Academic Press, London
    • (2003) ABC Proteins: From Bacteria to Man , pp. 3-35
    • Dassa, E.1
  • 2
    • 0036074018 scopus 로고    scopus 로고
    • Mammalian ABC transporters in health and disease
    • Borst, P. and Oude Elferink, R. P. (2002) Mammalian ABC transporters in health and disease. Annu. Rev. Biochem. 71, 537-592
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 537-592
    • Borst, P.1    Oude Elferink, R.P.2
  • 3
    • 0036176510 scopus 로고    scopus 로고
    • Mechanisms of cancer drug resistance
    • Gottesman, M. M. (2002) Mechanisms of cancer drug resistance. Annu. Rev. Med. 53, 615-627
    • (2002) Annu. Rev. Med. , vol.53 , pp. 615-627
    • Gottesman, M.M.1
  • 4
    • 0037457802 scopus 로고    scopus 로고
    • Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: An overview
    • Schinkel, A. H. and Jonker, J. W. (2003) Mammalian drug efflux transporters of the ATP binding cassette (ABC) family: an overview. Adv. Drug Deliv. Rev. 55, 3-29
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 3-29
    • Schinkel, A.H.1    Jonker, J.W.2
  • 5
  • 6
    • 0037046150 scopus 로고    scopus 로고
    • Proximity of bound Hoechst 33342 to the ATPase catalytic sites places the drug binding site of P-glycoprotein within the cytoplasmic membrane leaflet
    • Qu, Q. and Sharom, F. J. (2002) Proximity of bound Hoechst 33342 to the ATPase catalytic sites places the drug binding site of P-glycoprotein within the cytoplasmic membrane leaflet. Biochemistry 41, 4744-4752
    • (2002) Biochemistry , vol.41 , pp. 4744-4752
    • Qu, Q.1    Sharom, F.J.2
  • 7
    • 0036040835 scopus 로고    scopus 로고
    • Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors
    • Schumacher, M. A. and Brennan, R. G. (2002) Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors. Mol. Microbiol. 45, 885-893
    • (2002) Mol. Microbiol. , vol.45 , pp. 885-893
    • Schumacher, M.A.1    Brennan, R.G.2
  • 8
    • 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
  • 9
    • 0030995604 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein ATPase activity by beryllium fluoride
    • Sankaran, B., Bhagat, S. and Senior, A. E. (1997) Inhibition of P-glycoprotein ATPase activity by beryllium fluoride. Biochemistry 36, 6847-6853
    • (1997) Biochemistry , vol.36 , pp. 6847-6853
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 10
    • 0031148758 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein ATPase activity by procedures involving trapping of nucleotide in catalytic sites
    • Sankaran, B., Bhagat, S. and Senior, A. E. (1997) Inhibition of P-glycoprotein ATPase activity by procedures involving trapping of nucleotide in catalytic sites. Arch. Biochem. Biophys. 341, 160-169
    • (1997) Arch. Biochem. Biophys. , vol.341 , pp. 160-169
    • Sankaran, B.1    Bhagat, S.2    Senior, A.E.3
  • 11
    • 0028786395 scopus 로고
    • Both P-glycoprotein nucleotide-binding sites are catalytically active
    • Urbatsch, I. L., Sankaran, B., Bhagat, S. and Senior, A. E. (1995) Both P-glycoprotein nucleotide-binding sites are catalytically active. J. Biol. Chem. 270, 26956-26961
    • (1995) J. Biol. Chem. , vol.270 , pp. 26956-26961
    • Urbatsch, I.L.1    Sankaran, B.2    Bhagat, S.3    Senior, A.E.4
  • 12
  • 13
    • 0032821236 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: Towards a functional architecture
    • Jones, P. M. and George, A. M. (1999) Subunit interactions in ABC transporters: towards a functional architecture. FEMS Microbiol. Lett. 179, 187-202
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 187-202
    • Jones, P.M.1    George, A.M.2
  • 14
    • 33646557693 scopus 로고    scopus 로고
    • Nucleotide binding domain interactions during the mechanochemical reaction cycle of ATP-binding cassette transporters
    • Moody, J. E. and Thomas, P. J. (2005) Nucleotide binding domain interactions during the mechanochemical reaction cycle of ATP-binding cassette transporters. J. Bioenerg. Biomembr. 37, 475-479
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 475-479
    • Moody, J.E.1    Thomas, P.J.2
  • 15
    • 0034733677 scopus 로고    scopus 로고
    • Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sites
    • Loo, T. W. and Clarke, D. M. (2000) Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sites. J. Biol. Chem. 275, 19435-19438
    • (2000) J. Biol. Chem. , vol.275 , pp. 19435-19438
    • Loo, T.W.1    Clarke, D.M.2
  • 16
    • 0035814802 scopus 로고    scopus 로고
    • FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated
    • Qu, Q. and Sharom, F. J. (2001) FRET analysis indicates that the two ATPase active sites of the P-glycoprotein multidrug transporter are closely associated. Biochemistry 40, 1413-1422
    • (2001) Biochemistry , vol.40 , pp. 1413-1422
    • Qu, Q.1    Sharom, F.J.2
  • 17
    • 67650047300 scopus 로고    scopus 로고
    • Probing of conformational changes, catalytic cycle and ABC transporter function
    • (Holland, I. B., Kuchler, K., Higgins, C. and Cole, S. P., eds.), Academic Press, London
    • Sharom, F. J. (2003) Probing of conformational changes, catalytic cycle and ABC transporter function. In ABC Proteins: from Bacteria to Man (Holland, I. B., Kuchler, K., Higgins, C. and Cole, S. P., eds.), pp. 107-133, Academic Press, London
    • (2003) ABC Proteins: From Bacteria to Man , pp. 107-133
    • Sharom, F.J.1
  • 18
    • 0035782973 scopus 로고    scopus 로고
    • Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools
    • Sharom, F. J., Liu, R., Qu, Q. and Romsicki, Y. (2001) Exploring the structure and function of the P-glycoprotein multidrug transporter using fluorescence spectroscopic tools. Semin. Cell Dev. Biol. 12, 257-266
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 257-266
    • Sharom, F.J.1    Liu, R.2    Qu, Q.3    Romsicki, Y.4
  • 19
    • 0037432013 scopus 로고    scopus 로고
    • Transition state P-glycoprotein binds drugs and modulators with unchanged affinity, suggesting a concerted transport mechanism
    • Qu, Q., Chu, J. W. and Sharom, F. J. (2003) Transition state P-glycoprotein binds drugs and modulators with unchanged affinity, suggesting a concerted transport mechanism. Biochemistry 42, 1345-1353
    • (2003) Biochemistry , vol.42 , pp. 1345-1353
    • Qu, Q.1    Chu, J.W.2    Sharom, F.J.3
  • 20
    • 0037417765 scopus 로고    scopus 로고
    • Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle
    • Qu, Q., Russell, P. L. and Sharom, F. J. (2003) Stoichiometry and affinity of nucleotide binding to P-glycoprotein during the catalytic cycle. Biochemistry 42, 1170-1177
    • (2003) Biochemistry , vol.42 , pp. 1170-1177
    • Qu, Q.1    Russell, P.L.2    Sharom, F.J.3
  • 21
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II) · ADP · vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith, C. A. and Rayment, I. (1996) X-ray structure of the magnesium(II) · ADP · vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry 35, 5404-5417
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 26
    • 0030610719 scopus 로고    scopus 로고
    • 3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP
    • 3 mimics the transition state of protein phosphorylation in the crystal structure of nucleoside diphosphate kinase and MgADP. Proc. Natl. Acad. Sci. U.S.A. 94, 3579-3583
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3579-3583
    • Xu, Y.W.1    Morera, S.2    Janin, J.3    Cherfils, J.4
  • 28
    • 18644363550 scopus 로고    scopus 로고
    • Structure of the ABC transporter MsbA in complex with ADP · vanadate and lipopolysaccharide
    • Reyes, C. L. and Chang, G. (2005) Structure of the ABC transporter MsbA in complex with ADP · vanadate and lipopolysaccharide. Science (Washington, D.C.) 308, 1028-1031
    • (2005) Science (Washington, D.C.) , vol.308 , pp. 1028-1031
    • Reyes, C.L.1    Chang, G.2
  • 29
    • 18644362391 scopus 로고    scopus 로고
    • Structural basis of energy transduction in the transport cycle of MsbA
    • Dong, J., Yang, G. and McHaourab, H. S. (2005) Structural basis of energy transduction in the transport cycle of MsbA. Science (Washington, D.C.) 308, 1023-1028
    • (2005) Science (Washington, D.C.) , vol.308 , pp. 1023-1028
    • Dong, J.1    Yang, G.2    McHaourab, H.S.3
  • 30
    • 0026202059 scopus 로고
    • Strategies for the purification of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Doige, C. A. and Sharom, F. J. (1991) Strategies for the purification of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Protein Expr. Purif. 2, 256-265
    • (1991) Protein Expr. Purif. , vol.2 , pp. 256-265
    • Doige, C.A.1    Sharom, F.J.2
  • 31
    • 0029840320 scopus 로고    scopus 로고
    • Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains
    • Liu, R. and Sharom, F. J. (1996) Site-directed fluorescence labeling of P-glycoprotein on cysteine residues in the nucleotide binding domains. Biochemistry 35, 11865-11873
    • (1996) Biochemistry , vol.35 , pp. 11865-11873
    • Liu, R.1    Sharom, F.J.2
  • 32
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0029027674 scopus 로고
    • Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Sharom, F. J., Yu, X., Chu, J. W. K. and Doige, C. A. (1995) Characterization of the ATPase activity of P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochem. J. 308, 381-390
    • (1995) Biochem. J. , vol.308 , pp. 381-390
    • Sharom, F.J.1    Yu, X.2    Chu, J.W.K.3    Doige, C.A.4
  • 36
    • 0034610402 scopus 로고    scopus 로고
    • Intrinsic fluorescence of the P-glycoprotein multidrug transporter: Sensitivity of tryptophan residues to binding of drugs and nucleotides
    • Liu, R., Siemiarczuk, A. and Sharom, F. J. (2000) Intrinsic fluorescence of the P-glycoprotein multidrug transporter: sensitivity of tryptophan residues to binding of drugs and nucleotides. Biochemistry 39, 14927-14938
    • (2000) Biochemistry , vol.39 , pp. 14927-14938
    • Liu, R.1    Siemiarczuk, A.2    Sharom, F.J.3
  • 39
    • 0031454955 scopus 로고    scopus 로고
    • Conformational changes of P-glycoprotein by nucleotide binding
    • Wang, G., Pincheira, R., Zhang, M. and Zhang, J. T. (1997) Conformational changes of P-glycoprotein by nucleotide binding. Biochem. J. 328, 897-904
    • (1997) Biochem. J. , vol.328 , pp. 897-904
    • Wang, G.1    Pincheira, R.2    Zhang, M.3    Zhang, J.T.4
  • 40
    • 0034681959 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity
    • Julien, M. and Gros, P. (2000) Nucleotide-induced conformational changes in P-glycoprotein and in nucleotide binding site mutants monitored by trypsin sensitivity. Biochemistry 39, 4559-4568
    • (2000) Biochemistry , vol.39 , pp. 4559-4568
    • Julien, M.1    Gros, P.2
  • 41
    • 0030973613 scopus 로고    scopus 로고
    • Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter
    • Liu, R. and Sharom, F. J. (1997) Fluorescence studies on the nucleotide binding domains of the P-glycoprotein multidrug transporter. Biochemistry 36, 2836-2843
    • (1997) Biochemistry , vol.36 , pp. 2836-2843
    • Liu, R.1    Sharom, F.J.2
  • 42
    • 12144262818 scopus 로고    scopus 로고
    • Interaction of LDS-751 with P-glycoprotein and mapping of the location of the R drug binding site
    • 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
    • (2005) Biochemistry , vol.44 , pp. 643-655
    • Lugo, M.R.1    Sharom, F.J.2
  • 43
    • 0028097634 scopus 로고
    • Transmembrane aromatic amino acid distribution in P-glycoprotein. A functional role in broad substrate specificity
    • Pawagi, A. B., Wang, J., Silverman, M., Reithmeier, R. A. and Deber, C. M. (1994) Transmembrane aromatic amino acid distribution in P-glycoprotein. A functional role in broad substrate specificity. J. Mol. Biol. 235, 554-564
    • (1994) J. Mol. Biol. , vol.235 , pp. 554-564
    • Pawagi, A.B.1    Wang, J.2    Silverman, M.3    Reithmeier, R.A.4    Deber, C.M.5
  • 44
    • 0032492724 scopus 로고    scopus 로고
    • Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state
    • Ramachandra, M., Ambudkar, S. V., Chen, D., Hrycyna, C. A., Dey, S., Gottesman, M. M. and Pastan, I. (1998) Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state. Biochemistry 37, 5010-5019
    • (1998) Biochemistry , vol.37 , pp. 5010-5019
    • Ramachandra, M.1    Ambudkar, S.V.2    Chen, D.3    Hrycyna, C.A.4    Dey, S.5    Gottesman, M.M.6    Pastan, I.7
  • 46
    • 0043032667 scopus 로고    scopus 로고
    • Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
    • Chen, M., Abele, R. and Tampé, R. (2003) Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing. J. Biol. Chem. 278, 29686-29692
    • (2003) J. Biol. Chem. , vol.278 , pp. 29686-29692
    • Chen, M.1    Abele, R.2    Tampé, R.3
  • 47
    • 21744431708 scopus 로고    scopus 로고
    • Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1)
    • Payen, L., Gao, M., Westlake, C., Theis, A., Cole, S. P. C. and Deeley, R. G. (2005) Functional interactions between nucleotide binding domains and leukotriene C4 binding sites of multidrug resistance protein 1 (ABCC1). Mol. Pharmacol. 67, 1944-1953
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1944-1953
    • Payen, L.1    Gao, M.2    Westlake, C.3    Theis, A.4    Cole, S.P.C.5    Deeley, R.G.6
  • 48
    • 0037663389 scopus 로고    scopus 로고
    • P-glycoprotein catalytic mechanism - Studies of the ADP-vanadate inhibited state
    • Urbatsch, I. L., Tyndall, G. A., Tombline, G. and Senior, A. E. (2003) P-glycoprotein catalytic mechanism - studies of the ADP-vanadate inhibited state. J. Biol. Chem. 278, 23171-23179
    • (2003) J. Biol. Chem. , vol.278 , pp. 23171-23179
    • Urbatsch, I.L.1    Tyndall, G.A.2    Tombline, G.3    Senior, A.E.4
  • 49
    • 0035877703 scopus 로고    scopus 로고
    • 32P]diphosphate-trapped transition state intermediates of human P-glycoprotein are generated in the absence and presence of ATP hydrolysis
    • 32P]diphosphate-trapped transition state intermediates of human P-glycoprotein are generated in the absence and presence of ATP hydrolysis. J. Biol. Chem. 276, 21199-21208
    • (2001) J. Biol. Chem. , vol.276 , pp. 21199-21208
    • Sauna, Z.E.1    Smith, M.M.2    Müller, M.3    Ambudkar, S.V.4
  • 50
    • 0034460877 scopus 로고    scopus 로고
    • Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis
    • Sharma, S. and Davidson, A. L. (2000) Vanadate-induced trapping of nucleotides by purified maltose transport complex requires ATP hydrolysis. J. Bacteriol. 182, 6570-6576
    • (2000) J. Bacteriol. , vol.182 , pp. 6570-6576
    • Sharma, S.1    Davidson, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.