메뉴 건너뛰기




Volumn 45, Issue 13, 2006, Pages 4231-4239

Role of conserved prolines in the structure and function of the Na +/dicarboxylate cotransporter 1, NaDC1

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BIOLOGICAL MEMBRANES; MUTAGENS; ORGANIC ACIDS; PROTEINS; SODIUM COMPOUNDS;

EID: 33645541874     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052064y     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 0034194526 scopus 로고    scopus 로고
    • Molecular properties of sodium/dicarboxylate cotransporters
    • Pajor, A. M. (2000) Molecular properties of sodium/dicarboxylate cotransporters, J. Membr. Biol. 175, 1-8.
    • (2000) J. Membr. Biol. , vol.175 , pp. 1-8
    • Pajor, A.M.1
  • 2
    • 0033607213 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of SUT-1, a sulfate transporter from human high endothelial venules
    • Girard, J. P., Baekkevold, E. S., Feliu, J., Brandtzaeg, P., and Amalric, F. (1999) Molecular cloning and functional analysis of SUT-1, a sulfate transporter from human high endothelial venules, Proc. Natl. Acad. Sci. U.S.A. 96, 12772-12777.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12772-12777
    • Girard, J.P.1    Baekkevold, E.S.2    Feliu, J.3    Brandtzaeg, P.4    Amalric, F.5
  • 4
    • 0033027174 scopus 로고    scopus 로고
    • Citrate transport by the kidney and intestine
    • Pajor, A. M. (1999) Citrate transport by the kidney and intestine, Semin. Nephrol. 19, 195-200.
    • (1999) Semin. Nephrol. , vol.19 , pp. 195-200
    • Pajor, A.M.1
  • 5
    • 0034671596 scopus 로고    scopus 로고
    • Extended life-span conferred by cotransporter gene mutations in Drosophila
    • Rogina, B., Reenan, R. A., Nilsen, S. P., and Helfand, S. L. (2000) Extended life-span conferred by cotransporter gene mutations in Drosophila, Science 290, 2137-2140.
    • (2000) Science , vol.290 , pp. 2137-2140
    • Rogina, B.1    Reenan, R.A.2    Nilsen, S.P.3    Helfand, S.L.4
  • 6
    • 0030475519 scopus 로고    scopus 로고
    • +-dicarboxylate cotransporter using aritifusion protein antibodies
    • +-dicarboxylate cotransporter using aritifusion protein antibodies, Am. J. Physiol. 271, C1808-C1816.
    • (1996) Am. J. Physiol. , vol.271
    • Pajor, A.M.1    Sun, N.2
  • 7
    • 0035831095 scopus 로고    scopus 로고
    • +/dicarboxylate cotransporter: The N-terminus and hydrophilic loop 4 are located intracellularly
    • +/dicarboxylate cotransporter: The N-terminus and hydrophilic loop 4 are located intracellularly, Biochim. Biophys. Acta 1511, 80-89.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 80-89
    • Zhang, F.F.1    Pajor, A.M.2
  • 9
    • 0025602520 scopus 로고
    • The influence of proline residues on α-helical structure
    • Woolfson, D. N., and Williams, D. H. (1990) The influence of proline residues on α-helical structure, FEBS Lett. 277, 185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 10
    • 0035366669 scopus 로고    scopus 로고
    • Proline residues in two tightly coupled helices of the sulphate transporter, SHST1, are important for sulphate transport
    • 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.
    • (2001) Biochem. J. , vol.356 , pp. 589-594
    • Shelden, M.C.1    Loughlin, P.2    Tierney, M.L.3    Howitt, S.M.4
  • 11
    • 0035957526 scopus 로고    scopus 로고
    • Proline residues in transmembrane α helices affect the folding of bacteriorhodopsin
    • Lu, H., Marti, T., and Booth, P. J. (2001) Proline residues in transmembrane α helices affect the folding of bacteriorhodopsin, J. Mol. Biol. 308, 437-446.
    • (2001) J. Mol. Biol. , vol.308 , pp. 437-446
    • Lu, H.1    Marti, T.2    Booth, P.J.3
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: The role of prolines in signalling via transmembrane α-helices
    • Sansom, M. S., and 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
  • 15
  • 17
    • 0028957041 scopus 로고
    • Sequence and functional characterization of a renal sodium/dicarboxylate cotransporter
    • Pajor, A. M. (1995) Sequence and functional characterization of a renal sodium/dicarboxylate cotransporter, J. Biol. Chem. 270, 5779-5785.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5779-5785
    • Pajor, A.M.1
  • 18
    • 0035839457 scopus 로고    scopus 로고
    • +/dicarboxylate cotransporter
    • +/dicarboxylate cotransporter, J. Biol. Chem. 276, 29961-29968.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29961-29968
    • Pajor, A.M.1
  • 19
    • 12344273080 scopus 로고    scopus 로고
    • The "transport specificity ratio": A structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysis
    • King, S. C. (2004) The "transport specificity ratio": A structure-function tool to search the protein fold for loci that control transition state stability in membrane transport catalysis, BMC Biochem. 5, 16.
    • (2004) BMC Biochem. , vol.5 , pp. 16
    • King, S.C.1
  • 20
    • 0346843109 scopus 로고    scopus 로고
    • Use of the transport specificity ratio and cysteine-scanning mutagenesis to detect multiple substrate specificity determinants in the consensus amphipathic region of the Escherichia coli GABA (γ-aminobutyric acid) transporter encoded by gabP
    • King, S. C., and Brown-Istvan, L. (2003) Use of the transport specificity ratio and cysteine-scanning mutagenesis to detect multiple substrate specificity determinants in the consensus amphipathic region of the Escherichia coli GABA (γ-aminobutyric acid) transporter encoded by gabP, Biochem. J. 376, 633-644.
    • (2003) Biochem. J. , vol.376 , pp. 633-644
    • King, S.C.1    Brown-Istvan, L.2
  • 21
    • 0142116214 scopus 로고    scopus 로고
    • Mutagenesis of the N-glycosylation site of hNaSi-1 reduces transport activity
    • Li, H., and Pajor, A. M. (2003) Mutagenesis of the N-glycosylation site of hNaSi-1 reduces transport activity, Am. J. Physiol. Cell Physiol. 285, C1188-C1196.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Li, H.1    Pajor, A.M.2
  • 23
    • 0032524048 scopus 로고    scopus 로고
    • Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones
    • Tamarappoo, B. K., and Verkman, A. S. (1998) Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones, J. Clin. Invest. 101, 2257-2267.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2257-2267
    • Tamarappoo, B.K.1    Verkman, A.S.2
  • 24
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J., and Thornton, J. M. (1988) Helix geometry in proteins, J. Mol. Biol. 201, 601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 25
    • 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
  • 26
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson, J. S., and Richardson, D. C. (1988) Amino acid preferences for specific locations at the ends of α helices, Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 27
    • 0025059332 scopus 로고
    • Conformational studies on peptides with proline in the right-handed α-helical region
    • Sankararamakrishnan, R., and Vishveshwara, S. (1990) Conformational studies on peptides with proline in the right-handed α-helical region, Biopolymers 30, 287-298.
    • (1990) Biopolymers , vol.30 , pp. 287-298
    • Sankararamakrishnan, R.1    Vishveshwara, S.2
  • 28
    • 0346118860 scopus 로고    scopus 로고
    • Gating of Shaker-type, channels requires the flexibility of S6 caused by prolines
    • Labro, A. J., Raes, A. L., Bellens, I., Ottschytsch, N., and Snyders, D. J. (2003) Gating of Shaker-type, channels requires the flexibility of S6 caused by prolines, J. Biol. Chem. 278, 50724-50731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50724-50731
    • Labro, A.J.1    Raes, A.L.2    Bellens, I.3    Ottschytsch, N.4    Snyders, D.J.5
  • 29
    • 0034117176 scopus 로고    scopus 로고
    • Dopamine transporter proline mutations influence dopamine uptake, cocaine analog recognition, and expression
    • Lin, Z., Itokawa, M., and Uhl, G. R. (2000) Dopamine transporter proline mutations influence dopamine uptake, cocaine analog recognition, and expression, FASEB J. 14, 715-728.
    • (2000) FASEB J. , vol.14 , pp. 715-728
    • Lin, Z.1    Itokawa, M.2    Uhl, G.R.3
  • 30
    • 0346102599 scopus 로고    scopus 로고
    • Role of proline residues in the expression and function of the human noradrenaline transporter
    • Paczkowski, F. A., and Bryan-Lluka, L. J. (2004) Role of proline residues in the expression and function of the human noradrenaline transporter, J. Neurochem. 88, 203-211.
    • (2004) J. Neurochem. , vol.88 , pp. 203-211
    • Paczkowski, F.A.1    Bryan-Lluka, L.J.2
  • 32
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H. R., and Iwata, S. (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    Iwata, S.6
  • 33
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato, S., Ward, C. L., Krouse, M. E., Wine, J. J., and Kopito, R. R. (1996) Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation, J. Biol. Chem. 271, 635-638.
    • (1996) J. Biol. Chem. , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 34
    • 2442598041 scopus 로고    scopus 로고
    • Effects of chemical chaperones on partially retarded NaCl cotransporter mutants associated with Gitelman's syndrome in a mouse cortical collecting duct cell line
    • de Jong, J. C., Willems, P. H., Goossens, M., Vandewalle, A., van den Heuvel, L. P., Knoers, N. V., and Bindels, R. J. (2004) Effects of chemical chaperones on partially retarded NaCl cotransporter mutants associated with Gitelman's syndrome in a mouse cortical collecting duct cell line, Nephrol., Dial., Transplant. 19, 1069-1076.
    • (2004) Nephrol., Dial., Transplant. , vol.19 , pp. 1069-1076
    • De Jong, J.C.1    Willems, P.H.2    Goossens, M.3    Vandewalle, A.4    Van Den Heuvel, L.P.5    Knoers, N.V.6    Bindels, R.J.7
  • 35
    • 0033833911 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal organization, and functional characterization of a sodium-dicarboxylate cotransporter from mouse kidney
    • Pajor, A. M., and Sun, N. N. (2000) Molecular cloning, chromosomal organization, and functional characterization of a sodium-dicarboxylate cotransporter from mouse kidney, Am. J. Physiol. Renal. Physiol. 279, F482-F490.
    • (2000) Am. J. Physiol. Renal. Physiol. , vol.279
    • Pajor, A.M.1    Sun, N.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.