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Volumn 75, Issue 2, 2009, Pages 397-406

Multiple roles of charged amino acids in cytoplasmic loop 7 for expression and function of the multidrug and organic anion transporter MRP1 (ABCC1)

Author keywords

[No Author keywords available]

Indexed keywords

MULTIDRUG RESISTANCE PROTEIN 1;

EID: 59449105325     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.108.052860     Document Type: Article
Times cited : (23)

References (46)
  • 2
    • 0034502842 scopus 로고    scopus 로고
    • Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1)
    • Bakos E, Evers R, Calenda G, Tusnády GE, SzakácsG, Váradi A, and Sarkadi B (2000) Characterization of the amino-terminal regions in the human multidrug resistance protein (MRP1). J Cell Sci 113:4451-4461.
    • (2000) J Cell Sci , vol.113 , pp. 4451-4461
    • Bakos, E.1    Evers, R.2    Calenda, G.3    Tusnády, G.E.4    Szakács, G.5    Váradi, A.6    Sarkadi, B.7
  • 3
    • 11844297796 scopus 로고    scopus 로고
    • Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas
    • Conseil G, Deeley RG, and Cole SPC (2005) Role of two adjacent cytoplasmic tyrosine residues in MRP1 (ABCC1) transport activity and sensitivity to sulfonylureas. Biochem Pharmacol 69:451-461.
    • (2005) Biochem Pharmacol , vol.69 , pp. 451-461
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.C.3
  • 4
    • 31844446751 scopus 로고    scopus 로고
    • Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1)
    • Conseil G, Deeley RG, and Cole SPC (2006) Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1). J Biol Chem 281:43-50.
    • (2006) J Biol Chem , vol.281 , pp. 43-50
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.C.3
  • 5
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmem-brane conductance regulator
    • Cotten JF, Ostedgaard LS, Carson MR, and Welsh MJ (1996) Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmem-brane conductance regulator. JBiol Chem 271:21279-21284.
    • (1996) JBiol Chem , vol.271 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson, M.R.3    Welsh, M.J.4
  • 6
    • 0029944981 scopus 로고    scopus 로고
    • Detection ofa de novo R1066H mutation in an Italian patient affected by cystic fibrosis
    • Cremonesi L, Cainarca S, Rossi A, Padoan R, and Ferrari M (1996) Detection ofa de novo R1066H mutation in an Italian patient affected by cystic fibrosis. Hum Genet 98:119 -121.
    • (1996) Hum Genet , vol.98 , pp. 119-121
    • Cremonesi, L.1    Cainarca, S.2    Rossi, A.3    Padoan, R.4    Ferrari, M.5
  • 7
    • 0345299165 scopus 로고    scopus 로고
    • Drug resistance and ATP-dependent conjugate transport mediated by the apical multidrug resistance protein, MRP2, permanently expressed in human and canine cells
    • Cui Y, König J, Buchholz JK, Spring H, Leier I, and Keppler D (1999) Drug resistance and ATP-dependent conjugate transport mediated by the apical multidrug resistance protein, MRP2, permanently expressed in human and canine cells. Mol Pharmacol 55:929-937.
    • (1999) Mol Pharmacol , vol.55 , pp. 929-937
    • Cui, Y.1    König, J.2    Buchholz, J.K.3    Spring, H.4    Leier, I.5    Keppler, D.6
  • 8
    • 0035424958 scopus 로고    scopus 로고
    • Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation
    • Cui L, Hou YX, Riordan JR, and Chang XB (2001) Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation. Arch Biochem Biophys 392:153-161.
    • (2001) Arch Biochem Biophys , vol.392 , pp. 153-161
    • Cui, L.1    Hou, Y.X.2    Riordan, J.R.3    Chang, X.B.4
  • 9
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson RJ and Locher KP (2006) Structure of a bacterial multidrug ABC transporter. Nature 443:180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 10
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson RJ and Locher KP (2007) Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 581:935-938.
    • (2007) FEBS Lett , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 11
    • 33745835398 scopus 로고    scopus 로고
    • Transmembrane transport ofendo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins
    • Deeley RG, Westlake C, and Cole SPC (2006) Transmembrane transport ofendo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. Physiol Rev 86:849 -899.
    • (2006) Physiol Rev , vol.86 , pp. 849-899
    • Deeley, R.G.1    Westlake, C.2    Cole, S.P.C.3
  • 13
    • 11444266284 scopus 로고    scopus 로고
    • The AF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du K, Sharma M, and Lukacs GL (2005) The AF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat Struct Mol Biol 12:17-25.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 14
    • 0039184138 scopus 로고    scopus 로고
    • Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis
    • Falcón-Pérez JM, Mazón MJ, Molano J, and Eraso P (1999) Functional domain analysis of the yeast ABC transporter Ycf1p by site-directed mutagenesis. J Biol Chem 274:23584-23590.
    • (1999) J Biol Chem , vol.274 , pp. 23584-23590
    • Falcón-Pérez, J.M.1    Mazón, M.J.2    Molano, J.3    Eraso, P.4
  • 15
    • 0026780584 scopus 로고
    • Molecular characterization of cystic fibrosis: 16 novel mutations identified by analysis of the whole cystic fibrosis conductance transmem- brane regulator (CFTR) coding regions and splice site junctions
    • Fanen P, Ghanem N, Vidaud M, Besmond C, Martin J, Costes B, Plassa F, and Goossens M (1992) Molecular characterization of cystic fibrosis: 16 novel mutations identified by analysis of the whole cystic fibrosis conductance transmem- brane regulator (CFTR) coding regions and splice site junctions. Genomics 13:770-776.
    • (1992) Genomics , vol.13 , pp. 770-776
    • Fanen, P.1    Ghanem, N.2    Vidaud, M.3    Besmond, C.4    Martin, J.5    Costes, B.6    Plassa, F.7    Goossens, M.8
  • 16
    • 0030731950 scopus 로고    scopus 로고
    • Cystic fibrosis phenotype associated with pancreatic insufficiency does not always reflect the cAMP-dependent chloride conductive pathway defect. Analysis of C225R-CFTR and R1066C-CFTR
    • Fanen P, Labarthe R, Garnier F, Benharouga M, Goossens M, and Edelman A (1997) Cystic fibrosis phenotype associated with pancreatic insufficiency does not always reflect the cAMP-dependent chloride conductive pathway defect. Analysis of C225R-CFTR and R1066C-CFTR. J Biol Chem 272:30563- 30566.
    • (1997) J Biol Chem , vol.272 , pp. 30563-30566
    • Fanen, P.1    Labarthe, R.2    Garnier, F.3    Benharouga, M.4    Goossens, M.5    Edelman, A.6
  • 19
    • 0036828695 scopus 로고    scopus 로고
    • Charged amino acids in the sixth transmembrane helixofmultidrugresistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity
    • Haimeur A, Deeley RG, and Cole SPC (2002) Charged amino acids in the sixth transmembrane helixofmultidrugresistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity. J Biol Chem 277:41326-41333.
    • (2002) J Biol Chem , vol.277 , pp. 41326-41333
    • Haimeur, A.1    Deeley, R.G.2    Cole, S.P.C.3
  • 20
    • 2442660256 scopus 로고    scopus 로고
    • Mutations ofcharged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1)
    • Haimeur A, Conseil G, Deeley RG, and Cole SPC (2004) Mutations ofcharged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1). Mol Pharmacol 65:1375-1385.
    • (2004) Mol Pharmacol , vol.65 , pp. 1375-1385
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.C.4
  • 21
    • 0029987631 scopus 로고    scopus 로고
    • Location of a protease-hypersensitive region in the multidrug resistance protein (MRP) by mapping of the epitope of MRP-specific monoclonal antibody QCRL-1
    • Hipfner DR, Almquist KC, Stride BD, Deeley RG, and Cole SPC (1996) Location of a protease-hypersensitive region in the multidrug resistance protein (MRP) by mapping of the epitope of MRP-specific monoclonal antibody QCRL-1. Cancer Res 56:3307-3314.
    • (1996) Cancer Res , vol.56 , pp. 3307-3314
    • Hipfner, D.R.1    Almquist, K.C.2    Stride, B.D.3    Deeley, R.G.4    Cole, S.P.C.5
  • 22
    • 0030863293 scopus 로고    scopus 로고
    • Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic terminus
    • Hipfner DR, Almquist KC, Leslie EM, Gerlach JH, Grant CE, Deeley RG, and Cole SPC (1997) Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic terminus. J Biol Chem 272:23623-23630.
    • (1997) J Biol Chem , vol.272 , pp. 23623-23630
    • Hipfner, D.R.1    Almquist, K.C.2    Leslie, E.M.3    Gerlach, J.H.4    Grant, C.E.5    Deeley, R.G.6    Cole, S.P.C.7
  • 23
    • 0035844142 scopus 로고    scopus 로고
    • Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport
    • Ito K, Olsen SL, Qiu W, Deeley RG, and Cole SPC (2001) Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport. J Biol Chem 276:15616-15624.
    • (2001) J Biol Chem , vol.276 , pp. 15616-15624
    • Ito, K.1    Olsen, S.L.2    Qiu, W.3    Deeley, R.G.4    Cole, S.P.C.5
  • 24
    • 0042009288 scopus 로고    scopus 로고
    • 2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): Effects on protein expression, membrane localization, and transport function
    • 2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function. Biochim Biophys Acta 1615:103-114.
    • (2003) Biochim Biophys Acta , vol.1615 , pp. 103-114
    • Ito, K.1    Weigl, K.E.2    Deeley, R.G.3    Cole, S.P.C.4
  • 25
    • 0032562137 scopus 로고    scopus 로고
    • Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein
    • Kast C and Gros P (1998) Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein. Biochemistry 37:2305-2313.
    • (1998) Biochemistry , vol.37 , pp. 2305-2313
    • Kast, C.1    Gros, P.2
  • 26
    • 1242267914 scopus 로고    scopus 로고
    • Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions
    • Koike K, Conseil G, Leslie EM, Deeley RG, and Cole SP (2004) Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions. J Biol Chem 279:12325-12336.
    • (2004) J Biol Chem , vol.279 , pp. 12325-12336
    • Koike, K.1    Conseil, G.2    Leslie, E.M.3    Deeley, R.G.4    Cole, S.P.5
  • 29
    • 0013016426 scopus 로고    scopus 로고
    • Bioflavonoid stimulation ofglutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1)
    • Leslie EM, Deeley RG, and Cole SPC (2003b) Bioflavonoid stimulation ofglutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Drug Metab Dispos 31:11-15.
    • (2003) Drug Metab Dispos , vol.31 , pp. 11-15
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 30
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: Role of P-glycoprotein, MRP1, MRP2 and BCRP (ABCG2) in tissue defense
    • Leslie EM, Deeley RG, and Cole SPC (2005) Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2 and BCRP (ABCG2) in tissue defense. Toxicol Appl Pharmacol 204:216-237.
    • (2005) Toxicol Appl Pharmacol , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 31
    • 23444447815 scopus 로고    scopus 로고
    • Functional characterization of non-synonymous single nucleotide polymorphisms in the gene encoding human multidrug resistance protein 1 (MRP1/ABCC1)
    • Letourneau IJ, Deeley RG, and Cole SPC (2005) Functional characterization of non-synonymous single nucleotide polymorphisms in the gene encoding human multidrug resistance protein 1 (MRP1/ABCC1). Pharmacogenet Genomics 15:647-657.
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 647-657
    • Letourneau, I.J.1    Deeley, R.G.2    Cole, S.P.C.3
  • 32
    • 40949146910 scopus 로고    scopus 로고
    • Role of proline 1150 in functional interactions between the membrane spanning domains and nucleotide binding domains ofthe MRP1 (ABCC1) transporter
    • Letourneau IJ, Nakajima A, Deeley RG, and Cole SPC (2008) Role of proline 1150 in functional interactions between the membrane spanning domains and nucleotide binding domains ofthe MRP1 (ABCC1) transporter. Biochem Pharmacol 75:1659-1669.
    • (2008) Biochem Pharmacol , vol.75 , pp. 1659-1669
    • Letourneau, I.J.1    Nakajima, A.2    Deeley, R.G.3    Cole, S.P.C.4
  • 33
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporters architecture and mechanism
    • Locher KP, Lee AT, and Rees DC (2002) The E. coli BtuCD structure: a framework for ABC transporters architecture and mechanism. Science 296:1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 34
    • 0030009305 scopus 로고    scopus 로고
    • 4 and chemotherapeutic agents in membrane vesicles: Demonstration ofglutathione- dependent vincristine transport
    • 4 and chemotherapeutic agents in membrane vesicles: demonstration ofglutathione- dependent vincristine transport. J Biol Chem 271:9675-9682.
    • (1996) J Biol Chem , vol.271 , pp. 9675-9682
    • Loe, D.W.1    Almquist, K.C.2    Deeley, R.G.3    Cole, S.P.C.4
  • 36
    • 38349125066 scopus 로고    scopus 로고
    • Building an understanding of cystic fibrosis on the foundation of ABC transporter structures
    • Mendoza JL and Thomas PJ (2007) Building an understanding of cystic fibrosis on the foundation of ABC transporter structures. J Bioenerg Biomembr 39:499 -505.
    • (2007) J Bioenerg Biomembr , vol.39 , pp. 499-505
    • Mendoza, J.L.1    Thomas, P.J.2
  • 37
    • 0037031316 scopus 로고    scopus 로고
    • Evidence for the role of glycosylation in accessibility of the extracellular domains of human MRP1 (ABCC1)
    • Müller M, Yong M, Peng XH, Petre B, Arora S, and Ambudkar SV (2002) Evidence for the role of glycosylation in accessibility of the extracellular domains of human MRP1 (ABCC1). Biochemistry 41:10123-10132.
    • (2002) Biochemistry , vol.41 , pp. 10123-10132
    • Müller, M.1    Yong, M.2    Peng, X.H.3    Petre, B.4    Arora, S.5    Ambudkar, S.V.6
  • 38
    • 0141755312 scopus 로고    scopus 로고
    • Role ofcarboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)
    • Payen LF, Gao M, Westlake CJ, Cole SP, and Deeley RG (2003) Role ofcarboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1). JBiol Chem 278:38537-38547.
    • (2003) JBiol Chem , vol.278 , pp. 38537-38547
    • Payen, L.F.1    Gao, M.2    Westlake, C.J.3    Cole, S.P.4    Deeley, R.G.5
  • 40
    • 0034705145 scopus 로고    scopus 로고
    • Pseudoxanthomaelasticum: Mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter
    • Ringpfeil F, Lebwohl MG, Christiano AM, and Uitto J (2000) Pseudoxanthomaelasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter. Proc Natl Acad Sci U S A 97:6001-6006.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6001-6006
    • Ringpfeil, F.1    Lebwohl, M.G.2    Christiano, A.M.3    Uitto, J.4
  • 41
    • 0035853686 scopus 로고    scopus 로고
    • Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes
    • Sauna ZE and Ambudkar SV (2001) Characterization of the catalytic cycle of ATP hydrolysis by human P-glycoprotein. The two ATP hydrolysis events in a single catalytic cycle are kinetically similar but affect different functional outcomes. J Biol Chem 276:11653-11661.
    • (2001) J Biol Chem , vol.276 , pp. 11653-11661
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 42
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity
    • Seibert FS, Linsdell P, Loo TW, Hanrahan JW, Clarke DM, and Riordan JR (1996)Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity. J Biol Chem 271:15139-15145.
    • (1996) J Biol Chem , vol.271 , pp. 15139-15145
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordan, J.R.6
  • 43
    • 4644278479 scopus 로고    scopus 로고
    • Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): Glutamate 1204 is important for both the expression and catalytic activity of the transporter
    • Situ D, Haimeur A, Conseil G, Sparks KE, Zhang D, Deeley RG, and Cole SPC (2004) Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter. J Biol Chem 279:38871-38880.
    • (2004) J Biol Chem , vol.279 , pp. 38871-38880
    • Situ, D.1    Haimeur, A.2    Conseil, G.3    Sparks, K.E.4    Zhang, D.5    Deeley, R.G.6    Cole, S.P.C.7
  • 44
    • 0344629891 scopus 로고    scopus 로고
    • Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3
    • Westlake CJ, Qian YM, Gao M, Vasa M, Cole SP, and Deeley RG (2003) Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3. Biochemistry 42:14099 -14113.
    • (2003) Biochemistry , vol.42 , pp. 14099-14113
    • Westlake, C.J.1    Qian, Y.M.2    Gao, M.3    Vasa, M.4    Cole, S.P.5    Deeley, R.G.6
  • 45
    • 0028858490 scopus 로고
    • Intracellular loop between transmem-brane segments IV and V of cystic fibrosis transmembrane conductance regulator is involved in regulation of chloride channel conductance state
    • Xie J, Drumm ML, Ma J, and Davis PB (1995) Intracellular loop between transmem-brane segments IV and V of cystic fibrosis transmembrane conductance regulator is involved in regulation of chloride channel conductance state. J Biol Chem 270:28084-28091.
    • (1995) J Biol Chem , vol.270 , pp. 28084-28091
    • Xie, J.1    Drumm, M.L.2    Ma, J.3    Davis, P.B.4
  • 46
    • 38349065419 scopus 로고    scopus 로고
    • The hydroxyl group ofS685 in Walker A motif and the carboxyl group of D792 in Walker B motifofNBD1 play a crucial role for multidrug resistance protein folding and function
    • Yang R, Scavetta R, and Chang XB (2008) The hydroxyl group ofS685 in Walker A motif and the carboxyl group of D792 in Walker B motifofNBD1 play a crucial role for multidrug resistance protein folding and function. Biochim Biophys Acta 1778: 454-465.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 454-465
    • Yang, R.1    Scavetta, R.2    Chang, X.B.3


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