메뉴 건너뛰기




Volumn 151, Issue 12, 2010, Pages 5941-5951

Evidence of evolutionary conservation of function between the thyroxine transporter Oatp1c1 and major facilitator superfamily members

Author keywords

[No Author keywords available]

Indexed keywords

ORGANIC ANION TRANSPORTER; ORGANIC ANION TRANSPORTER 1; ORGANIC ANION TRANSPORTING POLYPEPTIDE 1C1; PROTEIN G399A; PROTEIN G399L; PROTEIN G409A; PROTEIN G409L; PROTEIN P609A; PROTEIN R601S; PROTEIN W277A; PROTEIN W277F; PROTEIN W278A; PROTEIN W278F; UNCLASSIFIED DRUG;

EID: 78649881896     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2010-0640     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0037427972 scopus 로고    scopus 로고
    • The superfamily of organic anion transporting polypeptides
    • Hagenbuch B, Meier PJ 2003 The superfamily of organic anion transporting polypeptides. Biochim Biophys Acta 1609:1-18
    • (2003) Biochim Biophys Acta , vol.1609 , pp. 1-18
    • Hagenbuch, B.1    Meier, P.J.2
  • 4
    • 0242384851 scopus 로고    scopus 로고
    • Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: High affinity transporter for thyroxine
    • Sugiyama D, Kusuhara H, Taniguchi H, Ishikawa S, Nozaki Y, Aburatani H, Sugiyama Y 2003 Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: high affinity transporter for thyroxine. J Biol Chem 278:43489-43495
    • (2003) J Biol Chem , vol.278 , pp. 43489-43495
    • Sugiyama, D.1    Kusuhara, H.2    Taniguchi, H.3    Ishikawa, S.4    Nozaki, Y.5    Aburatani, H.6    Sugiyama, Y.7
  • 5
    • 4344581457 scopus 로고    scopus 로고
    • Involvement of multispecific organic anion transporter, Oatp14 (Slc21a14), in the transport of thyroxine across the blood-brain barrier
    • Tohyama K, Kusuhara H, Sugiyama Y 2004 Involvement of multispecific organic anion transporter, Oatp14 (Slc21a14), in the transport of thyroxine across the blood-brain barrier. Endocrinology 145:4384-4391
    • (2004) Endocrinology , vol.145 , pp. 4384-4391
    • Tohyama, K.1    Kusuhara, H.2    Sugiyama, Y.3
  • 6
    • 34249981138 scopus 로고    scopus 로고
    • Cellular entry of thyroid hormones by organic anion transporting polypeptides
    • Hagenbuch B 2007 Cellular entry of thyroid hormones by organic anion transporting polypeptides. Best Pract Res 21:209-221
    • (2007) Best Pract Res , vol.21 , pp. 209-221
    • Hagenbuch, B.1
  • 7
    • 48749112588 scopus 로고    scopus 로고
    • Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family
    • Hagenbuch B, Gui C 2008 Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family. Xenobiotica 38:778-801
    • (2008) Xenobiotica , vol.38 , pp. 778-801
    • Hagenbuch, B.1    Gui, C.2
  • 8
    • 70350279309 scopus 로고    scopus 로고
    • The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics
    • Westholm DE, Salo DR, Viken KJ, Rumbley JN, Anderson GW 2009 The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics. Endocrinology 150:5153-5162
    • (2009) Endocrinology , vol.150 , pp. 5153-5162
    • Westholm, D.E.1    Salo, D.R.2    Viken, K.J.3    Rumbley, J.N.4    Anderson, G.W.5
  • 9
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • (New York, NY)
    • Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S 2003 Structure and mechanism of the lactose permease of Escherichia coli. Science (New York, NY) 301:610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 10
    • 33646442476 scopus 로고    scopus 로고
    • Organic anion transporting polypeptides of the OATP/SLCO superfamily: Identification of new members in nonmammalian species, comparative modeling and a potential transport mode
    • Meier-Abt F, Mokrab Y, Mizuguchi K 2005 Organic anion transporting polypeptides of the OATP/SLCO superfamily: identification of new members in nonmammalian species, comparative modeling and a potential transport mode. J Membr Biol 208:213-227
    • (2005) J Membr Biol , vol.208 , pp. 213-227
    • Meier-Abt, F.1    Mokrab, Y.2    Mizuguchi, K.3
  • 11
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • (New York, NY)
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN 2003 Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science (New York, NY) 301:616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 12
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • (New York, NY)
    • Yin Y, He X, Szewczyk P, Nguyen T, Chang G 2006 Structure of the multidrug transporter EmrD from Escherichia coli. Science (New York, NY) 312:741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 13
    • 59649083811 scopus 로고    scopus 로고
    • Competitive inhibition of organic anion transporting polypeptide 1c1-mediated thyroxine transport by the fenamate class of nonsteroidal antiinflammatory drugs
    • Westholm DE, Stenehjem DD, Rumbley JN, Drewes LR, Anderson GW 2009 Competitive inhibition of organic anion transporting polypeptide 1c1-mediated thyroxine transport by the fenamate class of nonsteroidal antiinflammatory drugs. Endocrinology 150:1025-1032
    • (2009) Endocrinology , vol.150 , pp. 1025-1032
    • Westholm, D.E.1    Stenehjem, D.D.2    Rumbley, J.N.3    Drewes, L.R.4    Anderson, G.W.5
  • 14
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Towards accurate multiple sequence alignments of distantly related proteins
    • (Oxford, England)
    • Pei J, Grishin NV 2007 PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics (Oxford, England) 23:802-808
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2
  • 15
    • 0036557845 scopus 로고    scopus 로고
    • Basic charge clusters and predictions of membrane protein topology
    • Juretić D, Zoranić L, Zucić D 2002 Basic charge clusters and predictions of membrane protein topology. J Chem Inf Comput Sci 42:620-632
    • (2002) J Chem Inf Comput Sci , vol.42 , pp. 620-632
    • Juretić, D.1    Zoranić, L.2    Zucić, D.3
  • 16
    • 0347093547 scopus 로고    scopus 로고
    • TM or not TM: Transmembrane protein prediction with low false positive rate using DAS-TMfilter
    • (Oxford, England)
    • Cserzo M, Eisenhaber F, Eisenhaber B, Simon I 2004 TM or not TM: transmembrane protein prediction with low false positive rate using DAS-TMfilter. Bioinformatics (Oxford, England) 20:136-137
    • (2004) Bioinformatics , vol.20 , pp. 136-137
    • Cserzo, M.1    Eisenhaber, F.2    Eisenhaber, B.3    Simon, I.4
  • 17
    • 0041620242 scopus 로고    scopus 로고
    • BPROMPT: A consensus server for membrane protein prediction
    • Taylor PD, Attwood TK, Flower DR 2003 BPROMPT: a consensus server for membrane protein prediction. Nucleic Acids Res 31:3698-3700
    • (2003) Nucleic Acids Res , vol.31 , pp. 3698-3700
    • Taylor, P.D.1    Attwood, T.K.2    Flower, D.R.3
  • 18
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • (Oxford, England)
    • Jones DT 2007 Improving the accuracy of transmembrane protein topology prediction using evolutionary information. Bioinformatics (Oxford, England) 23:538-544
    • (2007) Bioinformatics , vol.23 , pp. 538-544
    • Jones, D.T.1
  • 19
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • (Oxford, England)
    • Tusnády GE, Simon I 2001 The HMMTOP transmembrane topology prediction server. Bioinformatics (Oxford, England) 17:849-850
    • (2001) Bioinformatics , vol.17 , pp. 849-850
    • Tusnády, G.E.1    Simon, I.2
  • 20
    • 33847155026 scopus 로고    scopus 로고
    • Algorithms for incorporating prior topological information in HMMs: Application to transmembrane proteins
    • Bagos PG, Liakopoulos TD, Hamodrakas SJ 2006 Algorithms for incorporating prior topological information in HMMs: application to transmembrane proteins. BMC Bioinformatics 7:189
    • (2006) BMC Bioinformatics , vol.7 , pp. 189
    • Bagos, P.G.1    Liakopoulos, T.D.2    Hamodrakas, S.J.3
  • 21
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll L, Krogh A, Sonnhammer EL 2004 A combined transmembrane topology and signal peptide prediction method. J Mol Biol 338:1027-1036
    • (2004) J Mol Biol , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 22
    • 29144483361 scopus 로고    scopus 로고
    • An HMM posterior decoder for sequence feature prediction that includes homology information
    • (Oxford, England)
    • Kall L, Krogh A, Sonnhammer EL 2005 An HMM posterior decoder for sequence feature prediction that includes homology information. Bioinformatics (Oxford, England) 21(Suppl 1):i251-i257
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 23
    • 0034518145 scopus 로고    scopus 로고
    • T(E)Xtopo: Shaded membrane protein topology plots in LAT(E)X2epsilon
    • (Oxford, England)
    • Beitz E 2000 T(E)Xtopo: shaded membrane protein topology plots in LAT(E)X2epsilon. Bioinformatics (Oxford, England) 16:1050-1051
    • (2000) Bioinformatics , vol.16 , pp. 1050-1051
    • Beitz, E.1
  • 24
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL 1993 Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 25
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei J, Kim BH, Grishin NV 2008 PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36:2295-2300
    • (2008) Nucleic Acids Res , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 27
    • 34447253999 scopus 로고    scopus 로고
    • Sugar transport across lactose permease probed by steered molecular dynamics
    • Jensen MØ, Yin Y, Tajkhorshid E, Schulten K 2007 Sugar transport across lactose permease probed by steered molecular dynamics. Biophys J 93:92-102
    • (2007) Biophys J , vol.93 , pp. 92-102
    • Jensen, M.Ø.1    Yin, Y.2    Tajkhorshid, E.3    Schulten, K.4
  • 28
    • 33947132573 scopus 로고    scopus 로고
    • Sugar binding in lactose permease: Anomeric state of a disaccharide influences binding structure
    • Klauda JB, Brooks BR 2007 Sugar binding in lactose permease: anomeric state of a disaccharide influences binding structure. J Mol Biol 367:1523-1534
    • (2007) J Mol Biol , vol.367 , pp. 1523-1534
    • Klauda, J.B.1    Brooks, B.R.2
  • 29
    • 70349588813 scopus 로고    scopus 로고
    • Structural basis of substrate selectivity in the glycerol-3-phosphate: Phosphate antiporter GlpT
    • Law CJ, Enkavi G, Wang DN, Tajkhorshid E 2009 Structural basis of substrate selectivity in the glycerol-3-phosphate: phosphate antiporter GlpT. Biophys J 97:1346-1353
    • (2009) Biophys J , vol.97 , pp. 1346-1353
    • Law, C.J.1    Enkavi, G.2    Wang, D.N.3    Tajkhorshid, E.4
  • 30
    • 0345863729 scopus 로고    scopus 로고
    • Drug binding domains of MRP1 (ABCC1) as revealed by photoaffinity labeling
    • Karwatsky JM, Georges E 2004 Drug binding domains of MRP1 (ABCC1) as revealed by photoaffinity labeling. Curr Med Chem 4:19-30
    • (2004) Curr Med Chem , vol.4 , pp. 19-30
    • Karwatsky, J.M.1    Georges, E.2
  • 32
    • 0035940473 scopus 로고    scopus 로고
    • Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA
    • Lewinson O, Bibi E 2001 Evidence for simultaneous binding of dissimilar substrates by the Escherichia coli multidrug transporter MdfA. Biochemistry 40:12612-12618
    • (2001) Biochemistry , vol.40 , pp. 12612-12618
    • Lewinson, O.1    Bibi, E.2
  • 33
    • 0033524927 scopus 로고    scopus 로고
    • Bioenergetics of the staphylococcal multidrug export protein QacA. Identification of distinct binding sites for monovalent and divalent cations
    • Mitchell BA, Paulsen IT, Brown MH, Skurray RA 1999 Bioenergetics of the staphylococcal multidrug export protein QacA. Identification of distinct binding sites for monovalent and divalent cations. J Biol Chem 274:3541-3548
    • (1999) J Biol Chem , vol.274 , pp. 3541-3548
    • Mitchell, B.A.1    Paulsen, I.T.2    Brown, M.H.3    Skurray, R.A.4
  • 34
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interaction sites
    • Putman M, Koole LA, van Veen HW, Konings WN 1999 The secondary multidrug transporter LmrP contains multiple drug interaction sites. Biochemistry 38:13900-13905
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putman, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 35
    • 1242272736 scopus 로고    scopus 로고
    • Organic anion transporting polypeptides of the OATP/ SLC21 family: Phylogenetic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties
    • Hagenbuch B, Meier PJ 2004 Organic anion transporting polypeptides of the OATP/ SLC21 family: phylogenetic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties. Pflugers Arch 447:653-665
    • (2004) Pflugers Arch , vol.447 , pp. 653-665
    • Hagenbuch, B.1    Meier, P.J.2
  • 37
    • 25444499137 scopus 로고    scopus 로고
    • Importance of the GP dipeptide of the antiporter motif and other membrane-embedded proline and glycine residues in tetracycline efflux protein Tet(L)
    • De Jesus M, Jin J, Guffanti AA, Krulwich TA 2005 Importance of the GP dipeptide of the antiporter motif and other membrane-embedded proline and glycine residues in tetracycline efflux protein Tet(L). Biochemistry 44:12896-12904
    • (2005) Biochemistry , vol.44 , pp. 12896-12904
    • De Jesus, M.1    Jin, J.2    Guffanti, A.A.3    Krulwich, T.A.4
  • 38
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane α-helices
    • Sansom MS, Weinstein H 2000 Hinges, swivels and switches: the role of prolines in signalling via transmembrane α-helices. Trends Pharmacol Sci 21:445-451
    • (2000) Trends Pharmacol Sci , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 40
    • 10644282958 scopus 로고    scopus 로고
    • Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter
    • Unkles SE, Rouch DA, Wang Y, Siddiqi MY, Glass AD, Kinghorn JR 2004 Two perfectly conserved arginine residues are required for substrate binding in a high-affinity nitrate transporter. Proc Natl Acad Sci USA 101:17549-17554
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17549-17554
    • Unkles, S.E.1    Rouch, D.A.2    Wang, Y.3    Siddiqi, M.Y.4    Glass, A.D.5    Kinghorn, J.R.6
  • 41
    • 58949104204 scopus 로고    scopus 로고
    • Helix dynamics in a membrane transport protein: Comparative simulations of the glycerol-3-phosphate transporter and its constituent helices
    • D'Rozario RS, Sansom MS 2008 Helix dynamics in a membrane transport protein: comparative simulations of the glycerol-3-phosphate transporter and its constituent helices. Mol Membr Biol 25:571-583
    • (2008) Mol Membr Biol , vol.25 , pp. 571-583
    • D'Rozario, R.S.1    Sansom, M.S.2
  • 46
    • 33747590985 scopus 로고    scopus 로고
    • Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1
    • Hänggi E, Grundschober AF, Leuthold S, Meier PJ, St-Pierre MV 2006 Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1. Mol Pharmacol 70:806-817
    • (2006) Mol Pharmacol , vol.70 , pp. 806-817
    • Hänggi, E.1    Grundschober, A.F.2    Leuthold, S.3    Meier, P.J.4    St-Pierre, M.V.5
  • 47
    • 50849142229 scopus 로고    scopus 로고
    • Amino acid residues in transmembrane domain 10 of organic anion transporting polypeptide 1B3 are critical for cholecystokinin octapeptide transport
    • Gui C, Hagenbuch B 2008 Amino acid residues in transmembrane domain 10 of organic anion transporting polypeptide 1B3 are critical for cholecystokinin octapeptide transport. Biochemistry 47:9090-9097
    • (2008) Biochemistry , vol.47 , pp. 9090-9097
    • Gui, C.1    Hagenbuch, B.2
  • 48
    • 70350474996 scopus 로고    scopus 로고
    • Role of transmembrane domain 10 for the function of organic anion transporting polypeptide 1B1
    • Gui C, Hagenbuch B 2009 Role of transmembrane domain 10 for the function of organic anion transporting polypeptide 1B1. Protein Sci 18:2298-2306
    • (2009) Protein Sci , vol.18 , pp. 2298-2306
    • Gui, C.1    Hagenbuch, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.