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Volumn 48, Issue 36, 2009, Pages 8528-8539

The cytosolic half of helix III forms the substrate exit route during permeation events of the sodium/bile acid cotransporter ASBT

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATING REAGENTS; BILE ACID; CHOLESTEROL HOMEOSTASIS; CYTOSOLIC; MEMBRANE PROTEINS; MOLECULAR MECHANISM; SEQUENCE ALIGNMENTS; STRUCTURAL IMPORTANCE; SUBSTRATE BINDING; SUBSTRATE KINETICS; SURFACE EXPRESSION; TRANSMEMBRANE HELICES; TRANSPORT ACTIVITY; TRANSPORT CYCLE;

EID: 70249083096     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900616w     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 21844436858 scopus 로고    scopus 로고
    • Enterohepatic transport of bile salts and genetics of cholestasis
    • DOI 10.1016/j.jhep.2005.03.017, PII S0168827805003077
    • Pauli-Magnus, C., Stieger, B., Meier, Y., Kullak-Ublick, G. A., and Meier, P. J. (2005) Enterohepatic transport of bile salts and genetics of cholestasis. J. Hepatol. 43, 342-357. (Pubitemid 40956889)
    • (2005) Journal of Hepatology , vol.43 , Issue.2 , pp. 342-357
    • Pauli-Magnus, C.1    Stieger, B.2    Meier, Y.3    Kullak-Ublick, G.A.4    Meier, P.J.5
  • 2
    • 0032567523 scopus 로고    scopus 로고
    • Bile acid uptake via the human apical sodium-bile acid cotransporter is electrogenic
    • Weinman, S. A., Carruth, M. W., and Dawson, P. A. (1998) Bile acid uptake via the human apical sodium-bile acid cotransporter is electrogenic. J. Biol. Chem. 273, 34691-34695.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34691-34695
    • Weinman, S.A.1    Carruth, M.W.2    Dawson, P.A.3
  • 3
    • 0037379362 scopus 로고    scopus 로고
    • Bile salt transporters: Molecular characterization, function, and regulation
    • Trauner, M., and Boyer, J. L. (2003) Bile salt transporters: molecular characterization, function, and regulation. Physiol. Rev. 83, 633-671. (Pubitemid 36378680)
    • (2003) Physiological Reviews , vol.83 , Issue.2 , pp. 633-671
    • Trauner, M.1    Boyer, J.L.2
  • 8
    • 3042662820 scopus 로고    scopus 로고
    • Inhibition of ileal bile acid transport lowers plasma cholesterol levels by inactivating hepatic farnesoid X receptor and stimulating cholesterol 7 alpha-hydroxylase
    • DOI 10.1016/j.metabol.2004.01.017, PII S0026049504001143
    • Li, H., Xu, G., Shang, Q., Pan, L., Shefer, S., Batta, A. K., Bollineni, J., Tint, G. S., Keller, B. T., and Salen, G. (2004) Inhibition of ileal bile acid transport lowers plasma cholesterol levels by inactivating hepatic farnesoid X receptor and stimulating cholesterol 7 alpha-hydroxylase. Metabolism 53, 927-932. (Pubitemid 38829470)
    • (2004) Metabolism: Clinical and Experimental , vol.53 , Issue.7 , pp. 927-932
    • Li, H.1    Xu, G.2    Shang, Q.3    Pan, L.4    Shefer, S.5    Batta, A.K.6    Bollineni, J.7    Tint, G.S.8    Keller, B.T.9    Salen, G.10
  • 9
    • 27744571909 scopus 로고    scopus 로고
    • SC-435, an ileal apical sodium-codependent bile acid transporter inhibitor alters mRNA levels and enzyme activities of selected genes involved in hepatic cholesterol and lipoprotein metabolism in guinea pigs
    • DOI 10.1016/j.jnutbio.2005.06.009, PII S0955286305001865
    • West, K. L., McGrane, M., Odom, D., Keller, B., and Fernandez, M. L. (2005) SC-435, an ileal apical sodium-codependent bile acid transporter inhibitor alters mRNA levels and enzyme activities of selected genes involved in hepatic cholesterol and lipoprotein metabolism in guinea pigs. J. Nutr. Biochem. 16, 722-728. (Pubitemid 41630606)
    • (2005) Journal of Nutritional Biochemistry , vol.16 , Issue.12 , pp. 722-728
    • West, K.L.1    McGrane, M.2    Odom, D.3    Keller, B.4    Luz Fernandez, M.5
  • 10
    • 0036783669 scopus 로고    scopus 로고
    • 1-[4-[4-[(4R,5R)-3,3-Dibutyl-7-(dimethylamino)-2,3,4,5-tetrahydro-4- hydroxy-1,1-dioxido-1-benzothiepin-5-yl]phenoxy]butyl]-4-aza-1-azoniabicyclo[2. 2.2]octane methanesulfonate (SC-435), an ileal apical sodium-codependent bile acid transporter inhibitor alters hepatic cholesterol metabolism and lowers plasma low-density lipoprotein-cholesterol concentrations in guinea pigs
    • West, K. L., Ramjiganesh, T., Roy, S., Keller, B. T., and Fernandez, M. L. (2002) 1-[4-[4-[(4R,5R)-3,3-Dibutyl-7-(dimethylamino)-2,3,4,5-tetrahydro-4- hydroxy-1,1-dioxido-1-benzothiepin-5-yl]phenoxy]butyl]-4-aza-1-azoniabicyclo[2. 2.2]octane methanesulfonate (SC-435), an ileal apical sodium-codependent bile acid transporter inhibitor alters hepatic cholesterol metabolism and lowers plasma low-density lipoprotein-cholesterol concentrations in guinea pigs. J. Pharmacol. Exp. Ther. 303, 293-299.
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 293-299
    • West, K.L.1    Ramjiganesh, T.2    Roy, S.3    Keller, B.T.4    Fernandez, M.L.5
  • 11
    • 33745769730 scopus 로고    scopus 로고
    • Apical sodium dependent bile acid transporter (ASBT, SLC10A2): A potential prodrug target
    • DOI 10.1021/mp060022d
    • Balakrishnan, A., and Polli, J. E. (2006) Apical sodiumde pendent bile acid transporter (ASBT, SLC10A2): a potential prodrug target. Mol. Pharmaceutics 3, 223-230. (Pubitemid 44021430)
    • (2006) Molecular Pharmaceutics , vol.3 , Issue.3 , pp. 223-230
    • Balakrishnan, A.1    Polli, J.E.2
  • 12
    • 33745584351 scopus 로고    scopus 로고
    • Interaction of native bile acids with human apical sodium-dependent bile acid transporter (hASBT): Influence of steroidal hydroxylation pattern and C-24 conjugation
    • DOI 10.1007/s11095-006-0219-4
    • Balakrishnan, A., Wring, S. A., and Polli, J. E. (2006) Interaction of native bile acids with human apical sodium-dependent bile acid transporter (hASBT): influence of steroidal hydroxylation pattern and C-24 conjugation. Pharm. Res. 23, 1451-1459. (Pubitemid 43993808)
    • (2006) Pharmaceutical Research , vol.23 , Issue.7 , pp. 1451-1459
    • Balakrishnan, A.1    Wring, S.A.2    Polli, J.E.3
  • 13
    • 31044434123 scopus 로고    scopus 로고
    • Membrane topology of human ASBT (SLC10A2) determined by dual label epitope insertion scanning mutagenesis. New evidence for seven transmembrane domains
    • Banerjee, A., and Swaan, P. W. (2006) Membrane topology of human ASBT (SLC10A2) determined by dual label epitope insertion scanning mutagenesis. New evidence for seven transmembrane domains. Biochemistry 45, 943-953.
    • (2006) Biochemistry , vol.45 , pp. 943-953
    • Banerjee, A.1    Swaan, P.W.2
  • 14
    • 4444299420 scopus 로고    scopus 로고
    • Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2)
    • DOI 10.1021/bi049270a
    • Zhang, E. Y., Phelps, M. A., Banerjee, A., Khantwal, C. M., Chang, C., Helsper, F., and Swaan, P. W. (2004) Topology scanning and putative three-dimensional structure of the extracellular binding domains of the apical sodium-dependent bile acid transporter (SLC10A2). Biochemistry 43, 11380-11392. (Pubitemid 39186960)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11380-11392
    • Zhang, E.Y.1    Phelps, M.A.2    Banerjee, A.3    Khantwal, C.M.4    Chang, C.5    Helsper, F.6    Swaan, P.W.7
  • 16
    • 38549107239 scopus 로고    scopus 로고
    • Conformational flexibility of helix VI is essential for substrate permeation of the human apical sodium-dependent bile acid transporter
    • DOI 10.1124/mol.107.041640
    • Hussainzada, N., Khandewal, A., and Swaan, P. W. (2008) Conformational flexibility of helix VI is essential for substrate permeation of the human apical sodium-dependent bile acid transporter. Mol. Pharmacol. 73, 305-313. (Pubitemid 351159202)
    • (2008) Molecular Pharmacology , vol.73 , Issue.2 , pp. 305-313
    • Hussainzada, N.1    Khandewal, A.2    Swaan, P.W.3
  • 17
    • 33751290454 scopus 로고    scopus 로고
    • Transmembrane domain VII of the human apical sodium-dependent bile acid transporter ASBT (SLC10A2) lines the substrate translocation pathway
    • DOI 10.1124/mol.106.028647
    • Hussainzada, N., Banerjee, A., and Swaan, P. W. (2006) Transmembrane domain VII of the human apical sodium-dependent bile acid transporter ASBT (SLC10A2) lines the substrate translocation pathway. Mol. Pharmacol. 70, 1565-1574. (Pubitemid 44794211)
    • (2006) Molecular Pharmacology , vol.70 , Issue.5 , pp. 1565-1574
    • Hussainzada, N.1    Banerjee, A.2    Swaan, P.W.3
  • 18
    • 41149180595 scopus 로고    scopus 로고
    • Cytosolic half of transmembrane domain IV of the human bile acid transporter hASBT (SLC10A2) forms part of the substrate translocation pathway
    • Khantwal, C. M., and Swaan, P. W. (2008) Cytosolic half of transmembrane domain IV of the human bile acid transporter hASBT (SLC10A2) forms part of the substrate translocation pathway. Biochemistry 47, 3606-3614.
    • (2008) Biochemistry , vol.47 , pp. 3606-3614
    • Khantwal, C.M.1    Swaan, P.W.2
  • 21
    • 1542407805 scopus 로고    scopus 로고
    • Identification of a sodium-dependent organic anion transporter from rat adrenal gland
    • DOI 10.1016/j.bbrc.2004.02.048, PII S0006291X0400292X
    • Geyer, J., Godoy, J. R., and Petzinger, E. (2004) Identification of a sodium-dependent organic anion transporter from rat adrenal gland. Biochem. Biophys. Res. Commun. 316, 300-306. (Pubitemid 38338592)
    • (2004) Biochemical and Biophysical Research Communications , vol.316 , Issue.2 , pp. 300-306
    • Geyer, J.1    Godoy, J.R.2    Petzinger, E.3
  • 22
    • 33645119837 scopus 로고    scopus 로고
    • The solute carrier family SLC10: More than a family of bile acid transporters regarding function and phylogenetic relationships
    • Geyer, J., Wilke, T., and Petzinger, E. (2006) The solute carrier family SLC10: more than a family of bile acid transporters regarding function and phylogenetic relationships. Naunyn-Schmiedeberg's Arch. Pharmacol. 372, 413-431.
    • (2006) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.372 , pp. 413-431
    • Geyer, J.1    Wilke, T.2    Petzinger, E.3
  • 23
    • 0025602520 scopus 로고
    • The influence of proline residues on alpha-helical structure
    • Woolfson, D. N., and Williams, D. H. (1990) The influence of proline residues on alpha-helical structure. FEBS Lett. 277, 185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 24
    • 0035366669 scopus 로고    scopus 로고
    • Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate-transport
    • DOI 10.1042/0264-6021:3560589
    • Shelden, M. C., Loughlin, P., Tierney, M. L., and Howitt, S. M. (2001) Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport. Biochem. J. 356, 589-594. (Pubitemid 32532372)
    • (2001) Biochemical Journal , vol.356 , Issue.2 , pp. 589-594
    • Shelden, M.C.1    Loughlin, P.2    Tierney, M.L.3    Howitt, S.M.4
  • 25
    • 0035957526 scopus 로고    scopus 로고
    • Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin
    • DOI 10.1006/jmbi.2001.4605
    • Lu, H., Marti, T., and Booth, P. J. (2001) Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin. J. Mol. Biol. 308, 437-446. (Pubitemid 33043580)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.2 , pp. 437-446
    • Lu, H.1    Marti, T.2    Booth, P.J.3
  • 26
    • 0026537558 scopus 로고
    • Proline residues in transmembrane helices of channel and transport proteins: A molecular modelling study
    • Sansom, M. S. (1992) Proline residues in transmembrane helices of channel and transport proteins: a molecular modelling study. Protein Eng. 5, 53-60.
    • (1992) Protein Eng. , vol.5 , pp. 53-60
    • Sansom, M.S.1
  • 27
    • 0000882208 scopus 로고
    • Hypothesis about the function of membrane-buried proline residues in transport proteins
    • Brandl, C. J., and Deber, C. M. (1986) Hypothesis about the function of membrane-buried proline residues in transport proteins. Proc. Natl. Acad. Sci. U.S.A. 83, 917-921.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 917-921
    • Brandl, C.J.1    Deber, C.M.2
  • 28
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane alpha-helices
    • Sansom, M. S., and Weinstein, H. (2000) Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21, 445-451.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 29
    • 20544471895 scopus 로고    scopus 로고
    • Site-directed mutagenesis and use of bile acid-MTS conjugates to probe the role of cysteines in the human apical sodium-dependent bile acid transporter (SLC10A2)
    • DOI 10.1021/bi050553s
    • Banerjee, A., Ray, A., Chang, C., and Swaan, P. W. (2005) Site-directed mutagenesis and use of bile acid-MTS conjugates to probe the role of cysteines in the human apical sodium-dependent bile acid transporter (SLC10A2). Biochemistry 44, 8908-8917. (Pubitemid 40840457)
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8908-8917
    • Banerjee, A.1    Ray, A.2    Chang, C.3    Swaan, P.W.4
  • 30
    • 0029893370 scopus 로고    scopus 로고
    • Sinusoidal (basolateral) bile salt uptake systems of hepatocytes
    • Hagenbuch, B., and Meier, P. J. (1996) Sinusoidal (basolateral) bile salt uptake systems of hepatocytes. Semin. Liver Dis. 16, 129-136. (Pubitemid 26177625)
    • (1996) Seminars in Liver Disease , vol.16 , Issue.2 , pp. 129-136
    • Hagenbuch, B.1    Meier, P.J.2
  • 32
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes, F. S., Bright, J. N., and Sansom, M. S. (2002) Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323, 951-960.
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.3
  • 33
    • 33745194374 scopus 로고    scopus 로고
    • Identification of functionally relevant residues of the rat ileal apical sodium-dependent bile acid cotransporter
    • DOI 10.1074/jbc.M600034200
    • Sun, A. Q., Balasubramaniyan, N., Chen, H., Shahid, M., and Suchy, F. J. (2006) Identification of functionally relevant residues of the rat ileal apical sodium-dependent bile acid cotransporter. J. Biol. Chem. 281, 16410-16418. (Pubitemid 43909591)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.24 , pp. 16410-16418
    • Sun, A.-Q.1    Balasubramaniyan, N.2    Chen, H.3    Shahid, M.4    Suchy, F.J.5
  • 34
    • 0037351144 scopus 로고    scopus 로고
    • Transport of taurocholate by mutants of negatively charged amino acids, cysteines, and threonines of the rat liver sodium-dependent taurocholate cotransporting polypeptide Ntcp
    • DOI 10.1046/j.1432-1033.2003.03463.x
    • Zahner, D., Eckhardt, U., and Petzinger, E. (2003) Transport of taurocholate by mutants of negatively charged amino acids, cysteines, and threonines of the rat liver sodium-dependent taurocholate co-transporting polypeptide Ntcp. Eur. J. Biochem./FEBS 270, 1117-1127. (Pubitemid 36384445)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1117-1127
    • Zahner, D.1    Eckhardt, U.2    Petzinger, E.3
  • 35
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and Akabas, M. H. (1998) Substituted-cysteine accessibility method. Methods Enzymol. 293, 123-145.
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 36
    • 0032524637 scopus 로고    scopus 로고
    • Determination of external loop topology in the serotonin transporter by site-directed chemical labeling
    • DOI 10.1074/jbc.273.20.12675
    • Chen, J. G., Liu-Chen, S., and Rudnick, G. (1998) Determination of external loop topology in the serotonin transporter by site-directed chemical labeling. J. Biol. Chem. 273, 12675-12681. (Pubitemid 28240647)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.20 , pp. 12675-12681
    • Chen, J.-G.1    Liu-Chen, S.2    Rudnick, G.3
  • 37
    • 34247276092 scopus 로고    scopus 로고
    • Direct evidence that two cysteines in the dopamine transporter form a disulfide bond
    • DOI 10.1007/s11010-006-9348-7
    • Chen, R., Wei, H., Hill, E. R., Chen, L., Jiang, L., Han, D. D., and Gu, H. H. (2007) Direct evidence that two cysteines in the dopamine transporter form a disulfide bond. Mol. Cell. Biochem. 298, 41-48. (Pubitemid 46605282)
    • (2007) Molecular and Cellular Biochemistry , vol.298 , Issue.1-2 , pp. 41-48
    • Chen, R.1    Wei, H.2    Hill, E.R.3    Chen, L.4    Jiang, L.5    Han, D.D.6    Gu, H.H.7
  • 38
    • 0033681163 scopus 로고    scopus 로고
    • A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines
    • Seal, R. P., Leighton, B. H., and Amara, S. G. (2000) A model for the topology of excitatory amino acid transporters determined by the extracellular accessibility of substituted cysteines. Neuron 25, 695-706.
    • (2000) Neuron , vol.25 , pp. 695-706
    • Seal, R.P.1    Leighton, B.H.2    Amara, S.G.3
  • 40
    • 0038053899 scopus 로고    scopus 로고
    • Structural insights into the mechanism of proton pumping by bacteriorhodopsin
    • DOI 10.1016/S0014-5793(03)00386-7
    • Hirai, T., and Subramaniam, S. (2003) Structural insights into the mechanism of proton pumping by bacteriorhodopsin. FEBS Lett. 545, 2-8. (Pubitemid 36629629)
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 2-8
    • Hirai, T.1    Subramaniam, S.2
  • 41
    • 0036343993 scopus 로고    scopus 로고
    • Conformational dynamics of helix S6 from Shaker potassium channel: Simulation studies
    • Bright, J. N., Shrivastava, I. H., Cordes, F. S., and Sansom, M. S. (2002) Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies. Biopolymers 64, 303-313.
    • (2002) Biopolymers , vol.64 , pp. 303-313
    • Bright, J.N.1    Shrivastava, I.H.2    Cordes, F.S.3    Sansom, M.S.4
  • 42
    • 33645541874 scopus 로고    scopus 로고
    • +/dicarboxylate cotransporter 1, NaDC1
    • +/dicarboxylate cotransporter 1, NaDC1. Biochemistry 45, 4231-4239.
    • (2006) Biochemistry , vol.45 , pp. 4231-4239
    • Joshi, A.D.1    Pajor, A.M.2
  • 44
    • 0035427377 scopus 로고    scopus 로고
    • Proline-induced hinges in transmembrane helices: Possible roles in ion channel gating
    • Tieleman, D. P., Shrivastava, I. H., Ulmschneider, M. R., and Sansom, M. S. (2001) Proline-induced hinges in transmembrane helices: possible roles in ion channel gating. Proteins 44, 63-72.
    • (2001) Proteins , vol.44 , pp. 63-72
    • Tieleman, D.P.1    Shrivastava, I.H.2    Ulmschneider, M.R.3    Sansom, M.S.4
  • 45
    • 0032561347 scopus 로고    scopus 로고
    • Critical amino acid residues in transmembrane span 7 of the serotonin transporter identified by random mutagenesis
    • DOI 10.1074/jbc.273.43.28098
    • Penado, K. M., Rudnick, G., and Stephan, M. M. (1998) Critical amino acid residues in transmembrane span 7 of the serotonin transporter identified by random mutagenesis. J. Biol. Chem. 273, 28098-28106. (Pubitemid 28496105)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 28098-28106
    • Penado, K.M.Y.1    Rudnick, G.2    Stephan, M.M.3
  • 46
    • 0028866988 scopus 로고
    • Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity
    • Wong, M. H., Oelkers, P., and Dawson, P. A. (1995) Identification of a mutation in the ileal sodium-dependent bile acid transporter gene that abolishes transport activity. J. Biol. Chem. 270, 27228-27234.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27228-27234
    • Wong, M.H.1    Oelkers, P.2    Dawson, P.A.3


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