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Volumn 96, Issue 2, 2009, Pages 748-760

Effects on conformational states of the rabbit sodium/glucose cotransporter through modulation of polarity and charge at glutamine 457

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ORYCTOLAGUS CUNICULUS;

EID: 58849097168     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2008.09.045     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 0030070055 scopus 로고    scopus 로고
    • Defects in Na+/glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption
    • Martin, M. G., E. Turk, M. P. Lostao, C. Kerner, and E. M. Wright. 1996. Defects in Na+/glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption. Nat. Genet. 12:216-220.
    • (1996) Nat. Genet , vol.12 , pp. 216-220
    • Martin, M.G.1    Turk, E.2    Lostao, M.P.3    Kerner, C.4    Wright, E.M.5
  • 2
    • 55949115655 scopus 로고    scopus 로고
    • Revised immunolocalization of the Na+-D-glucose cotransporter SGLT1 in rat organs with an improved antibody
    • Balen, D., M. Ljubojevic, D. Breljak, H. Brzica, V. Zlender, et al. 2008. Revised immunolocalization of the Na+-D-glucose cotransporter SGLT1 in rat organs with an improved antibody. Am. J. Physiol. Cell Physiol. C475-C489.
    • (2008) Am. J. Physiol. Cell Physiol
    • Balen, D.1    Ljubojevic, M.2    Breljak, D.3    Brzica, H.4    Zlender, V.5
  • 3
    • 0032486248 scopus 로고    scopus 로고
    • Cholecystokinin decreases intestinal hexose absorption by a parallel reduction in SGLT1 abundance in the brush-border membrane
    • Hirsh, A. J., and C. I. Cheeseman. 1998. Cholecystokinin decreases intestinal hexose absorption by a parallel reduction in SGLT1 abundance in the brush-border membrane. J. Biol. Chem. 273:14545-14549.
    • (1998) J. Biol. Chem , vol.273 , pp. 14545-14549
    • Hirsh, A.J.1    Cheeseman, C.I.2
  • 4
    • 34447525464 scopus 로고    scopus 로고
    • Na+-D-glucose cotransporter in the kidney of Leucoraja erinacea: Molecular identification and intrarenal distribution
    • Althoff, T., H. Hentschel, J. Luig, H. Schutz, M. Kasch, et al. 2007. Na+-D-glucose cotransporter in the kidney of Leucoraja erinacea: molecular identification and intrarenal distribution. Am. J. Physiol. Regul. Integr. Comp. Physiol. 292:R2391-2399.
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.292
    • Althoff, T.1    Hentschel, H.2    Luig, J.3    Schutz, H.4    Kasch, M.5
  • 5
    • 0030924414 scopus 로고    scopus 로고
    • Membrane topology motifs in the SGLT cotransporter family
    • Turk, E., and E. M. Wright. 1997. Membrane topology motifs in the SGLT cotransporter family. J. Membr. Biol. 159:1-20.
    • (1997) J. Membr. Biol , vol.159 , pp. 1-20
    • Turk, E.1    Wright, E.M.2
  • 6
    • 0032491402 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of the segment between putative transmembrane helices IV and V of the high affinity Na+/Glucose cotransporter SGLT1. Evidence that this region participates in the Na+ and voltage dependence of the transporter
    • Lo, B., and M. Silverman. 1998. Cysteine scanning mutagenesis of the segment between putative transmembrane helices IV and V of the high affinity Na+/Glucose cotransporter SGLT1. Evidence that this region participates in the Na+ and voltage dependence of the transporter. J. Biol. Chem. 273:29341-29351.
    • (1998) J. Biol. Chem , vol.273 , pp. 29341-29351
    • Lo, B.1    Silverman, M.2
  • 8
    • 36749092724 scopus 로고    scopus 로고
    • D-Glucose-recognition and phlorizin-binding sites in human sodium/D-glucose cotransporter 1 (hSGLT1): A tryptophan scanning study
    • Tyagi, N. K., A. Kumar, P. Goyal, D. Pandey, W. Siess, et al. 2007. D-Glucose-recognition and phlorizin-binding sites in human sodium/D-glucose cotransporter 1 (hSGLT1): a tryptophan scanning study. Biochemistry. 46:13616-13628.
    • (2007) Biochemistry , vol.46 , pp. 13616-13628
    • Tyagi, N.K.1    Kumar, A.2    Goyal, P.3    Pandey, D.4    Siess, W.5
  • 9
    • 34047213359 scopus 로고    scopus 로고
    • Voltage-clamp fluorometry in the local environment of the C255-C511 disulfide bridge of the Na+/glucose cotransporter
    • Gagnon, D. G., C. Frindel, and J. Y. Lapointe. 2007. Voltage-clamp fluorometry in the local environment of the C255-C511 disulfide bridge of the Na+/glucose cotransporter. Biophys. J. 92:2403-2411.
    • (2007) Biophys. J , vol.92 , pp. 2403-2411
    • Gagnon, D.G.1    Frindel, C.2    Lapointe, J.Y.3
  • 10
    • 34548477177 scopus 로고    scopus 로고
    • Three surface subdomains form the vestibule of the Na+/glucose cotransporter SGLT1
    • Puntheeranurak, T., M. Kasch, X. Xia, P. Hinterdorfer, and R. K. Kinne. 2007. Three surface subdomains form the vestibule of the Na+/glucose cotransporter SGLT1. J. Biol. Chem. 282:25222-25230.
    • (2007) J. Biol. Chem , vol.282 , pp. 25222-25230
    • Puntheeranurak, T.1    Kasch, M.2    Xia, X.3    Hinterdorfer, P.4    Kinne, R.K.5
  • 11
    • 12344291860 scopus 로고    scopus 로고
    • Perturbation analysis of the voltage-sensitive conformational changes of the Na+/glucose cotransporter
    • Loo, D. D., B. A. Hirayama, A. Cha, F. Bezanilla, and E. M. Wright. 2005. Perturbation analysis of the voltage-sensitive conformational changes of the Na+/glucose cotransporter. J. Gen. Physiol. 125:13-36.
    • (2005) J. Gen. Physiol , vol.125 , pp. 13-36
    • Loo, D.D.1    Hirayama, B.A.2    Cha, A.3    Bezanilla, F.4    Wright, E.M.5
  • 12
    • 0037192171 scopus 로고    scopus 로고
    • Fluorescence studies of ligand-induced conformational changes of the Na(+)/glucose cotransporter
    • Meinild, A. K., B. A. Hirayama, E. M. Wright, and D. D. Loo. 2002. Fluorescence studies of ligand-induced conformational changes of the Na(+)/glucose cotransporter. Biochemistry. 41:1250-1258.
    • (2002) Biochemistry , vol.41 , pp. 1250-1258
    • Meinild, A.K.1    Hirayama, B.A.2    Wright, E.M.3    Loo, D.D.4
  • 13
    • 0035966086 scopus 로고    scopus 로고
    • Residue 457 controls sugar binding and transport in the Na(+)/glucose cotransporter
    • Diez-Sampedro, A., E. M. Wright, and B. A. Hirayama. 2001. Residue 457 controls sugar binding and transport in the Na(+)/glucose cotransporter. J. Biol. Chem. 276:49188-49194.
    • (2001) J. Biol. Chem , vol.276 , pp. 49188-49194
    • Diez-Sampedro, A.1    Wright, E.M.2    Hirayama, B.A.3
  • 14
  • 15
    • 0030817964 scopus 로고    scopus 로고
    • Five transmembrane helices form the sugar pathway through the Na+/glucose cotransporter
    • Panayotova-Heiermann, M., S. Eskandari, E. Turk, G. A. Zampighi, and E. M. Wright. 1997. Five transmembrane helices form the sugar pathway through the Na+/glucose cotransporter. J. Biol. Chem. 272:20324-20327.
    • (1997) J. Biol. Chem , vol.272 , pp. 20324-20327
    • Panayotova-Heiermann, M.1    Eskandari, S.2    Turk, E.3    Zampighi, G.A.4    Wright, E.M.5
  • 16
    • 3042731991 scopus 로고    scopus 로고
    • Position 170 of rabbit Na+/glucose cotransporter (rSGLT1) lies in the Na+ pathway; modulation of polarity/charge at this site regulates charge transfer and carrier turnover
    • Huntley, S. A., D. Krofchick, and M. Silverman. 2004. Position 170 of rabbit Na+/glucose cotransporter (rSGLT1) lies in the Na+ pathway; modulation of polarity/charge at this site regulates charge transfer and carrier turnover. Biophys. J. 87:295-310.
    • (2004) Biophys. J , vol.87 , pp. 295-310
    • Huntley, S.A.1    Krofchick, D.2    Silverman, M.3
  • 17
    • 0031974924 scopus 로고    scopus 로고
    • Replacement of Ala-166 with cysteine in the high affinity rabbit sodium/glucose transporter alters transport kinetics and allows methanethiosulfonate ethylamine to inhibit transporter function
    • Lo, B., and M. Silverman. 1998. Replacement of Ala-166 with cysteine in the high affinity rabbit sodium/glucose transporter alters transport kinetics and allows methanethiosulfonate ethylamine to inhibit transporter function. J. Biol. Chem. 273:903-909.
    • (1998) J. Biol. Chem , vol.273 , pp. 903-909
    • Lo, B.1    Silverman, M.2
  • 18
    • 0030783291 scopus 로고    scopus 로고
    • Sodium leak pathway and substrate binding order in the Na+-glucose cotransporter
    • Chen, X. Z., M. J. Coady, F. Jalal, B. Wallendorff, and J. Y. Lapointe. 1997. Sodium leak pathway and substrate binding order in the Na+-glucose cotransporter. Biophys. J. 73:2503-2510.
    • (1997) Biophys. J , vol.73 , pp. 2503-2510
    • Chen, X.Z.1    Coady, M.J.2    Jalal, F.3    Wallendorff, B.4    Lapointe, J.Y.5
  • 19
    • 34249843310 scopus 로고
    • Electrogenic properties of the cloned Na+/glucose cotransporter: I. Voltage-clamp studies
    • Parent, L., S. Supplisson, D. D. Loo, and E. M. Wright. 1992. Electrogenic properties of the cloned Na+/glucose cotransporter: I. Voltage-clamp studies. J. Membr. Biol. 125:49-62.
    • (1992) J. Membr. Biol , vol.125 , pp. 49-62
    • Parent, L.1    Supplisson, S.2    Loo, D.D.3    Wright, E.M.4
  • 20
    • 52749095703 scopus 로고    scopus 로고
    • Transmembrane IV of the high-affinity sodium-glucose cotransporter participates in sugar binding
    • Liu, T., B. Lo, P. Speight, and M. Silverman. 2008. Transmembrane IV of the high-affinity sodium-glucose cotransporter participates in sugar binding. Am. J. Physiol. Cell Physiol. 295:C64-C72.
    • (2008) Am. J. Physiol. Cell Physiol , vol.295
    • Liu, T.1    Lo, B.2    Speight, P.3    Silverman, M.4
  • 21
    • 0038778551 scopus 로고    scopus 로고
    • Investigating the conformational States of the rabbit na(+)/glucose cotransporter
    • Krofchick, D., and M. Silverman. 2003. Investigating the conformational States of the rabbit na(+)/glucose cotransporter. Biophys. J. 84:3690-3702.
    • (2003) Biophys. J , vol.84 , pp. 3690-3702
    • Krofchick, D.1    Silverman, M.2
  • 22
    • 33645670616 scopus 로고    scopus 로고
    • A glutamine to glutamate mutation at position 170 (Q170E) in the rabbit Na+/glucose cotransporter, rSGLT1, enhances binding affinity for Na+
    • Huntley, S. A., D. Krofchick, and M. Silverman. 2006. A glutamine to glutamate mutation at position 170 (Q170E) in the rabbit Na+/glucose cotransporter, rSGLT1, enhances binding affinity for Na+. Biochemistry. 45:4653-4663.
    • (2006) Biochemistry , vol.45 , pp. 4653-4663
    • Huntley, S.A.1    Krofchick, D.2    Silverman, M.3
  • 23
    • 33846444737 scopus 로고    scopus 로고
    • Effect of substrate on the pre-steady-state kinetics of the Na+/glucose cotransporter
    • Gagnon, D. G., C. Frindel, and J. Y. Lapointe. 2007. Effect of substrate on the pre-steady-state kinetics of the Na+/glucose cotransporter. Biophys. J. 92:461-472.
    • (2007) Biophys. J , vol.92 , pp. 461-472
    • Gagnon, D.G.1    Frindel, C.2    Lapointe, J.Y.3
  • 25
    • 0034779753 scopus 로고    scopus 로고
    • Common mechanisms of inhibition for the Na+/glucose (hSGLT1) and Na+/Cl-/GABA (hGAT1) cotransporters
    • Hirayama, B. A., A. Diez-Sampedro, and E. M. Wright. 2001. Common mechanisms of inhibition for the Na+/glucose (hSGLT1) and Na+/Cl-/GABA (hGAT1) cotransporters. Br. J. Pharmacol. 134:484-495.
    • (2001) Br. J. Pharmacol , vol.134 , pp. 484-495
    • Hirayama, B.A.1    Diez-Sampedro, A.2    Wright, E.M.3
  • 26
    • 0029861546 scopus 로고    scopus 로고
    • Fast voltage clamp discloses a new component of presteady-state currents from the Na(+)-glucose cotransporter
    • Chen, X. Z., M. J. Coady, and J. Y. Lapointe. 1996. Fast voltage clamp discloses a new component of presteady-state currents from the Na(+)-glucose cotransporter. Biophys. J. 71:2544-2552.
    • (1996) Biophys. J , vol.71 , pp. 2544-2552
    • Chen, X.Z.1    Coady, M.J.2    Lapointe, J.Y.3
  • 28
    • 0028169456 scopus 로고
    • Sodium/D-glucose cotransporter charge movements involve polar residues
    • Panayotova-Heiermann, M., D. D. Loo, M. P. Lostao, and E. M. Wright. 1994. Sodium/D-glucose cotransporter charge movements involve polar residues. J. Biol. Chem. 269:21016-21020.
    • (1994) J. Biol. Chem , vol.269 , pp. 21016-21020
    • Panayotova-Heiermann, M.1    Loo, D.D.2    Lostao, M.P.3    Wright, E.M.4
  • 29
    • 0942276396 scopus 로고    scopus 로고
    • Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding
    • Loland, C. J., C. Granas, J. A. Javitch, and U. Gether. 2004. Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding. J. Biol. Chem. 279:3228-3238.
    • (2004) J. Biol. Chem , vol.279 , pp. 3228-3238
    • Loland, C.J.1    Granas, C.2    Javitch, J.A.3    Gether, U.4
  • 30
    • 0042206767 scopus 로고    scopus 로고
    • Residues in the extracellular loop 4 are critical for maintaining the conformational equilibrium of the gamma-aminobutyric acid transporter-1
    • MacAulay, N., A. K. Meinild, T. Zeuthen, and U. Gether. 2003. Residues in the extracellular loop 4 are critical for maintaining the conformational equilibrium of the gamma-aminobutyric acid transporter-1. J. Biol. Chem. 278:28771-28777.
    • (2003) J. Biol. Chem , vol.278 , pp. 28771-28777
    • MacAulay, N.1    Meinild, A.K.2    Zeuthen, T.3    Gether, U.4
  • 31
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett, H. W., A. T. Lee, P. Lum, K. P. Locher, and D. C. Rees. 2007. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science. 315:373-377.
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 32
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., I. Smirnova, V. Kasho, G. Verner, H. R. Kaback, et al. 2003. Structure and mechanism of the lactose permease of Escherichia coli. Science. 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
  • 33
    • 31744434105 scopus 로고    scopus 로고
    • Identification of a disulfide bridge linking the fourth and the seventh extracellular-loops of the na+/glucose cotransporter
    • Gagnon, D. G., P. Bissonnette, and J. Y. Lapointe. 2006. Identification of a disulfide bridge linking the fourth and the seventh extracellular-loops of the na+/glucose cotransporter. J. Gen. Physiol. 127:145-158.
    • (2006) J. Gen. Physiol , vol.127 , pp. 145-158
    • Gagnon, D.G.1    Bissonnette, P.2    Lapointe, J.Y.3
  • 34
    • 34249840554 scopus 로고
    • Electrogenic properties of the cloned Na+/glucose cotransporter: II. A transport model under nonrapid equilibrium conditions
    • Parent, L., S. Supplisson, D. D. Loo, and E. M. Wright. 1992. Electrogenic properties of the cloned Na+/glucose cotransporter: II. A transport model under nonrapid equilibrium conditions. J. Membr. Biol. 125:63-79.
    • (1992) J. Membr. Biol , vol.125 , pp. 63-79
    • Parent, L.1    Supplisson, S.2    Loo, D.D.3    Wright, E.M.4


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