메뉴 건너뛰기




Volumn 109, Issue 28, 2012, Pages 11194-11199

Structure and permeation mechanism of a mammalian urea transporter

Author keywords

Channels; Membrane proteins; Osmosensing; Renal physiology

Indexed keywords

CARRIER PROTEIN; UNCLASSIFIED DRUG; UREA; UREA TRANSPORTER B;

EID: 84863944898     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1207362109     Document Type: Article
Times cited : (63)

References (59)
  • 3
    • 0037974519 scopus 로고    scopus 로고
    • Mammalian urea transporters
    • Sands JM (2003) Mammalian urea transporters. Annu Rev Physiol 65:543-566.
    • (2003) Annu Rev Physiol , vol.65 , pp. 543-566
    • Sands, J.M.1
  • 5
    • 84861678616 scopus 로고    scopus 로고
    • New insights into urea and glucose handling by the kidney, and the urine concentrating mechanism
    • Bankir L, Yang B (2012) New insights into urea and glucose handling by the kidney, and the urine concentrating mechanism. Kidney Int 81:1179-1198.
    • (2012) Kidney Int , vol.81 , pp. 1179-1198
    • Bankir, L.1    Yang, B.2
  • 7
    • 0037155920 scopus 로고    scopus 로고
    • Urea-selective concentrating defect in transgenic mice lacking urea transporter UT-B
    • DOI 10.1074/jbc.M200207200
    • Yang B, Bankir L, Gillespie A, Epstein CJ, Verkman AS (2002) Urea-selective concentrating defect in transgenic mice lacking urea transporter UT-B. J Biol Chem 277:10633-10637. (Pubitemid 34968188)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10633-10637
    • Yang, B.1    Bankir, L.2    Gillespie, A.3    Epstein, C.J.4    Verkman, A.S.5
  • 8
    • 0037184066 scopus 로고    scopus 로고
    • Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence for UT-B-facilitated water transport in erythrocytes
    • Yang B, Verkman AS (2002) Analysis of double knockout mice lacking aquaporin-1 and urea transporter UT-B. Evidence for UT-B-facilitated water transport in erythrocytes. J Biol Chem 277:36782-36786.
    • (2002) J Biol Chem , vol.277 , pp. 36782-36786
    • Yang, B.1    Verkman, A.S.2
  • 10
    • 82755177484 scopus 로고    scopus 로고
    • Role of thin descending limb urea transport in renal urea handling and the urine concentrating mechanism
    • Lei TL, et al. (2011) Role of thin descending limb urea transport in renal urea handling and the urine concentrating mechanism. Am J PhysiolRenal Physiol 301:F1251-F1259.
    • (2011) Am J PhysiolRenal Physiol , vol.301
    • Lei, T.L.1
  • 11
    • 23344432987 scopus 로고    scopus 로고
    • Impaired urea accumulation in the inner medulla of mice lacking the urea transporter UT-A2
    • DOI 10.1128/MCB.25.16.7357-7363.2005
    • Uchida S, et al. (2005) Impaired urea accumulation in the inner medulla of mice lacking the urea transporter UT-A2. Mol Cell Biol 25:7357-7363. (Pubitemid 41105930)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.16 , pp. 7357-7363
    • Uchida, S.1    Sohara, E.2    Rai, T.3    Ikawa, M.4    Okabe, M.5    Sasaki, S.6
  • 13
    • 80053958730 scopus 로고    scopus 로고
    • A genome-wide association study of bladder cancer identifies a new susceptibility locus within SLC14A1, a urea transporter gene on chromosome 18q12.3
    • Garcia-ClosasM, et al. (2011) A genome-wide association study of bladder cancer identifies a new susceptibility locus within SLC14A1, a urea transporter gene on chromosome 18q12.3. Hum Mol Genet 20:4282-4289.
    • (2011) Hum Mol Genet , vol.20 , pp. 4282-4289
    • Garcia-Closas, M.1
  • 14
    • 80053945781 scopus 로고    scopus 로고
    • European genome-wide association study identifies SLC14A1 as a new urinary bladder cancer susceptibility gene
    • Rafnar T, et al. (2011) European genome-wide association study identifies SLC14A1 as a new urinary bladder cancer susceptibility gene. Hum Mol Genet 20:4268-4281.
    • (2011) Hum Mol Genet , vol.20 , pp. 4268-4281
    • Rafnar, T.1
  • 15
    • 33646485107 scopus 로고    scopus 로고
    • Tissue distribution of UT-A and UT-B mRNA and protein in rat
    • Doran JJ, et al. (2006) Tissue distribution of UT-A and UT-B mRNA and protein in rat. Am J Physiol Regul Integr Comp Physiol 290:R1446-R1459.
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.290
    • Doran, J.J.1
  • 17
    • 33646485094 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites
    • Hoffert JD, Pisitkun T, Wang GH, Shen RF, Knepper MA (2006) Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites. Proc Natl Acad Sci USA 103:7159-7164.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7159-7164
    • Hoffert, J.D.1    Pisitkun, T.2    Wang, G.H.3    Shen, R.F.4    Knepper, M.A.5
  • 18
    • 0036079910 scopus 로고    scopus 로고
    • Vasopressin rapidly increases phosphorylation of UT-A1 urea transporter in rat IMCDs through PKA
    • Zhang C, Sands JM, Klein JD (2002) Vasopressin rapidly increases phosphorylation of UT-A1 urea transporter in rat IMCDs through PKA. Am J Physiol Renal Physiol 282:F85-F90. (Pubitemid 34654203)
    • (2002) American Journal of Physiology - Renal Physiology , vol.282 , Issue.1
    • Zhang, C.1    Sands, J.M.2    Klein, J.D.3
  • 19
    • 44949221250 scopus 로고    scopus 로고
    • Functional characterization of mouse urea transporters UT-A2 and UT-A3 expressed in purified Xenopus laevis oocyte plasma membranes
    • Maciver B, Smith CP, Hill WG, Zeidel ML (2008) Functional characterization of mouse urea transporters UT-A2 and UT-A3 expressed in purified Xenopus laevis oocyte plasma membranes. Am J Physiol Renal Physiol 294:F956-F964.
    • (2008) Am J Physiol Renal Physiol , vol.294
    • Maciver, B.1    Smith, C.P.2    Hill, W.G.3    Zeidel, M.L.4
  • 20
    • 0027403576 scopus 로고
    • Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial
    • Mannuzzu LM, Moronne MM, Macey RI (1993) Estimate of the number of urea transport sites in erythrocyte ghosts using a hydrophobic mercurial. J Membr Biol 133:85-97. (Pubitemid 23116350)
    • (1993) Journal of Membrane Biology , vol.133 , Issue.1 , pp. 85-97
    • Mannuzzu, L.M.1    Moronne, M.M.2    Macey, R.I.3
  • 21
    • 72049114961 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the kidney urea transporter
    • Levin EJ, Quick M, Zhou M (2009) Crystal structure of a bacterial homologue of the kidney urea transporter. Nature 462:757-761.
    • (2009) Nature , vol.462 , pp. 757-761
    • Levin, E.J.1    Quick, M.2    Zhou, M.3
  • 22
    • 0030097416 scopus 로고    scopus 로고
    • Tandem sequence repeats in urea transporters: Identification of an urea transporter signature sequence
    • Rousselet G, Ripoche P, Bailly P (1996) Tandem sequence repeats in urea transporters: Identification of an urea transporter signature sequence. Am J Physiol 270:F554-F555. (Pubitemid 126756491)
    • (1996) American Journal of Physiology , vol.270 , Issue.3 PART 2
    • Rousselet, G.1    Ripoche, P.2    Bailly, P.3
  • 23
    • 0347519333 scopus 로고    scopus 로고
    • The urea transporter (UT) family: Bioinformatic analyses leading to structural, functional, and evolutionary predictions
    • Minocha R, Studley K, Saier MH, Jr (2003) The urea transporter (UT) family: Bioinformatic analyses leading to structural, functional, and evolutionary predictions. Receptors Channels 9:345-352. (Pubitemid 38008221)
    • (2003) Receptors and Channels , vol.9 , Issue.6 , pp. 345-352
    • Minocha, R.1    Studley, K.2    Saier Jr., M.H.3
  • 25
    • 36549001229 scopus 로고    scopus 로고
    • Measurement of water and solute permeability by stopped-flow fluorimetry
    • DOI 10.1385/1-59745-519-9:323, Methods in Membrane Lipids
    • Mathai JC, Zeidel ML (2007) Measurement of water and solute permeability by stopped-flow fluorimetry. Methods Mol Biol 400:323-332. (Pubitemid 350183698)
    • (2007) Methods in Molecular Biology , vol.400 , pp. 323-332
    • Mathai, J.C.1    Zeidel, M.L.2
  • 26
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • DOI 10.1038/414872a
    • Sui H, Han BG, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878. (Pubitemid 34024731)
    • (2001) Nature , vol.414 , Issue.6866 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 27
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot BL, Grubmuller H (2001) Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GlpF. Science 294(5550):2353-2357.
    • (2001) Science , vol.294 , Issue.5550 , pp. 2353-2357
    • De Groot, B.L.1    Grubmuller, H.2
  • 33
    • 23044496908 scopus 로고    scopus 로고
    • What makes an aquaporin a glycerol channel? A comparative study of AqpZ and GlpF
    • DOI 10.1016/j.str.2005.05.005, PII S0969212605002054
    • Wang Y, Schulten K, Tajkhorshid E (2005) What makes an aquaporin a glycerol channel? A comparative study of AqpZ and GlpF. Structure 13:1107-1118. (Pubitemid 41111479)
    • (2005) Structure , vol.13 , Issue.8 , pp. 1107-1118
    • Wang, Y.1    Schulten, K.2    Tajkhorshid, E.3
  • 34
    • 62049085752 scopus 로고    scopus 로고
    • Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae
    • Raunser S, et al. (2009) Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae. J Mol Biol 387:619-627.
    • (2009) J Mol Biol , vol.387 , pp. 619-627
    • Raunser, S.1
  • 35
    • 34250172757 scopus 로고    scopus 로고
    • Comparative transport efficiencies of urea analogues through urea transporter UT-B
    • DOI 10.1016/j.bbamem.2007.04.010, PII S0005273607001460
    • Zhao D, Sonawane ND, Levin MH, Yang B (2007) Comparative transport efficiencies of urea analogues through urea transporter UT-B. Biochim Biophys Acta 1768:1815-1821. (Pubitemid 46900809)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.7 , pp. 1815-1821
    • Zhao, D.1    Sonawane, N.D.2    Levin, M.H.3    Yang, B.4
  • 37
    • 0032540009 scopus 로고    scopus 로고
    • Urea transpoter UT3 functions as an efficient water channel: Direct evidence for a common water/urea pathway
    • DOI 10.1074/jbc.273.16.9369
    • Yang B, Verkman AS (1998) Urea transporter UT3 functions as an efficient water channel. Direct evidence for a common water/urea pathway. J Biol Chem 273:9369-9372. (Pubitemid 28183015)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9369-9372
    • Yang, B.1    Verkman, A.S.2
  • 40
    • 0015406331 scopus 로고
    • Countercurrent multiplication system without active transport in inner medulla
    • Kokko JP, Rector FC, Jr (1972) Countercurrent multiplication system without active transport in inner medulla. Kidney Int 2:214-223.
    • (1972) Kidney Int , vol.2 , pp. 214-223
    • Kokko, J.P.1    Rector Jr., F.C.2
  • 41
    • 33947509228 scopus 로고    scopus 로고
    • Role of UTB urea transporters in the urine concentrating mechanism of the rat kidney
    • Layton AT (2007) Role of UTB urea transporters in the urine concentrating mechanism of the rat kidney. Bull Math Biol 69:887-929.
    • (2007) Bull Math Biol , vol.69 , pp. 887-929
    • Layton, A.T.1
  • 42
    • 0015385254 scopus 로고
    • Concentration of urine in a central core model of the renal counterflow system
    • Stephenson JL (1972) Concentration of urine in a central core model of the renal counterflow system. Kidney Int 2:85-94.
    • (1972) Kidney Int , vol.2 , pp. 85-94
    • Stephenson, J.L.1
  • 43
    • 0030845197 scopus 로고    scopus 로고
    • Evidence that aquaporin-1 mediates NaCl-induced water flux across descending vasa recta
    • Pallone TL, Kishore BK, Nielsen S, Agre P, Knepper MA (1997) Evidence that aquaporin-1 mediates NaCl-induced water flux across descending vasa recta. Am J Physiol 272:F587-F596.
    • (1997) Am J Physiol , vol.272
    • Pallone, T.L.1    Kishore, B.K.2    Nielsen, S.3    Agre, P.4    Knepper, M.A.5
  • 46
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66:213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 47
    • 0030841590 scopus 로고    scopus 로고
    • Collaborative computational project, number 4: Providing programs for protein crystallography
    • DOI 10.1016/S0076-6879(97)77034-4
    • Dodson EJ, Winn M, Ralph A (1997) Collaborative Computational Project, number 4: Providing programs for protein crystallography. Methods Enzymol 277:620-633. (Pubitemid 27390943)
    • (1997) Methods in Enzymology , vol.277 , pp. 620-633
    • Dodson, E.J.1    Winn, M.2    Ralph, A.3
  • 48
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62:439-450.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 49
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66:12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 51
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method
    • Kumar S, Bouzida D, Swendsen RH, Kollman PA, Rosenberg JM (1992) The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method. J Comput Chem 13:1011-1021.
    • (1992) J Comput Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Swendsen, R.H.3    Kollman, P.A.4    Rosenberg, J.M.5
  • 52
    • 0035277126 scopus 로고    scopus 로고
    • Extension to the weighted histogram analysis method: Combining umbrella sampling with free energy calculations
    • DOI 10.1016/S0010-4655(00)00215-0
    • Roux B, Souaille M (2001) Extension to the weighted histogram analysis method: Combining umbrella sampling with free energy calculations. Comput Phys Commun 135:40-57. (Pubitemid 32265281)
    • (2001) Computer Physics Communications , vol.135 , Issue.1 , pp. 40-57
    • Souaille, M.1    Roux, B.2
  • 53
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell AD, Feig M, Brooks CL (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 25:1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 54
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • MacKerell AD, et al. (2010) Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types. J Phys Chem B 114:7830-7843.
    • (2010) J Phys Chem B , vol.114 , pp. 7830-7843
    • MacKerell, A.D.1
  • 55
    • 0033134665 scopus 로고    scopus 로고
    • Structural details of urea binding to barnase: A molecular dynamics analysis
    • DOI 10.1016/S0969-2126(99)80064-1
    • Caflisch A, KarplusM (1999) Structural details of urea binding to barnase: A molecular dynamics analysis. Struct Fold Des 7:477-488. (Pubitemid 29230482)
    • (1999) Structure , vol.7 , Issue.5 , pp. 477-488
    • Caflisch, A.1    Karplus, M.2
  • 57
    • 36449007836 scopus 로고
    • Constant-pressure moleculardynamics simulation-the Langevin piston method
    • Feller SE, Zhang YH, Pastor RW, Brooks BR (1995) Constant-pressure moleculardynamics simulation-the Langevin piston method. J Chem Phys 103:4613-4621.
    • (1995) J Chem Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 58
    • 36449003554 scopus 로고
    • Constant-pressure molecular-dynamics algorithms
    • Martyna GJ, Tobias DJ, Klein ML (1994) Constant-pressure molecular-dynamics algorithms. J Chem Phys 101:4177-4189.
    • (1994) J Chem Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 59
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an N.Log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald-an N.Log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.