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Volumn 8, Issue 4, 2013, Pages

The Gating Mechanism of the Human Aquaporin 5 Revealed by Molecular Dynamics Simulations

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN 5; HISTIDINE; MONOMER; TETRAMER;

EID: 84875639205     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0059897     Document Type: Article
Times cited : (67)

References (69)
  • 2
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple amber force fields and development of improved protein backbone parameters
    • Hornak VR, Abel RA, Okur AB, Strockbine BA, Roitberg AC, et al. (2006) Comparison of multiple amber force fields and development of improved protein backbone parameters. Proteins 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.R.1    Abel, R.A.2    Okur, A.B.3    Strockbine, B.A.4    Roitberg, A.C.5
  • 3
    • 84855466022 scopus 로고    scopus 로고
    • Charge equilibration force fields for molecular dynamics simulations of lipids, bilayers, and integral membrane protein systems
    • Lucas TR, Bauer BA, Patel S, (2012) Charge equilibration force fields for molecular dynamics simulations of lipids, bilayers, and integral membrane protein systems. Biochimica et Biophysica Acta-Biomembranes 1818: 318-329.
    • (2012) Biochimica Et Biophysica Acta-Biomembranes , vol.1818 , pp. 318-329
    • Lucas, T.R.1    Bauer, B.A.2    Patel, S.3
  • 4
    • 0347089020 scopus 로고    scopus 로고
    • Energetics of ion conduction through the gramicidin channel
    • Allen TW, Andersen OS, Roux B, (2004) Energetics of ion conduction through the gramicidin channel. Proc Nat Acad Sci USA 101: 117-122.
    • (2004) Proc Nat Acad Sci USA , vol.101 , pp. 117-122
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 5
    • 57149107204 scopus 로고    scopus 로고
    • Calculating free-energy profiles in biomolecular systems from fast nonequilibrium processes
    • Forney MW, Janosi L, Kosztin I, (2008) Calculating free-energy profiles in biomolecular systems from fast nonequilibrium processes. Phys Rev E 78: 051913.
    • (2008) Phys Rev E , vol.78 , pp. 051913
    • Forney, M.W.1    Janosi, L.2    Kosztin, I.3
  • 6
    • 80855156716 scopus 로고    scopus 로고
    • Molecular simulation approaches to membrane proteins
    • Stansfeld PJ, Sansom MSP, (2011) Molecular simulation approaches to membrane proteins. Structure 19: 1562-1572.
    • (2011) Structure , vol.19 , pp. 1562-1572
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 8
    • 17044406611 scopus 로고    scopus 로고
    • The dynamics and energetics of water permeation and proton exclusion in aquaporins
    • de Groot BL, Grubmüller H, (2005) The dynamics and energetics of water permeation and proton exclusion in aquaporins. Current Opinion In Structural Biology 15: 176-183.
    • (2005) Current Opinion In Structural Biology , vol.15 , pp. 176-183
    • de Groot, B.L.1    Grubmüller, H.2
  • 9
    • 0034609808 scopus 로고    scopus 로고
    • Structural determinants of water permeation through aquaporin-1
    • Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, et al. (2000) Structural determinants of water permeation through aquaporin-1. Nature 407: 599-605.
    • (2000) Nature , vol.407 , pp. 599-605
    • Murata, K.1    Mitsuoka, K.2    Hirai, T.3    Walz, T.4    Agre, P.5
  • 10
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the aqp1 water channel
    • Sui H, Han BG, Lee JK, Walian P, Jap BK, (2001) Structural basis of water-specific transport through the aqp1 water channel. Nature 414: 872-8.
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 13
    • 0037331359 scopus 로고    scopus 로고
    • Role of aquaporin water channels in eye function
    • Verkman AS, (2003) Role of aquaporin water channels in eye function. Experimental Eye Research 76: 137-143.
    • (2003) Experimental Eye Research , vol.76 , pp. 137-143
    • Verkman, A.S.1
  • 14
    • 61449282195 scopus 로고    scopus 로고
    • Knock-Out Models Reveal New Aquaporin Functions, Verlag Berlin Heidelberg: Springer, volume 190 of Aquaporins
    • Verkman AS (2009) Knock-Out Models Reveal New Aquaporin Functions, Verlag Berlin Heidelberg: Springer, volume 190 of Aquaporins, Handbook of Experimental Pharmacology. pp.359-381.
    • (2009) Handbook of Experimental Pharmacology , pp. 359-381
    • Verkman, A.S.1
  • 15
    • 0026503030 scopus 로고
    • Appearance of water channels in xenopus oocytes expressing red-cell CHIP28 protein
    • Preston GM, Carroll TP, Guggino WB, Agre P, (1992) Appearance of water channels in xenopus oocytes expressing red-cell CHIP28 protein. Science 256: 385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 16
    • 0022448651 scopus 로고
    • Para-(chloromercuri)benzenesulfonate binding by membrane-proteins and the inhibition of water transport in human-erythrocytes
    • Benga G, Popescu O, Pop VI, Holmes RP, (1986) Para-(chloromercuri)benzenesulfonate binding by membrane-proteins and the inhibition of water transport in human-erythrocytes. Biochemistry 25: 1535-1538.
    • (1986) Biochemistry , vol.25 , pp. 1535-1538
    • Benga, G.1    Popescu, O.2    Pop, V.I.3    Holmes, R.P.4
  • 17
    • 0023610959 scopus 로고
    • Purification and partial characterization of the Mr 30,000 integral membrane-protein associated with the erythrocyte Rh(D) antigen
    • Agre PP, Saboori AM, Asimos A, Smith BL, (1987) Purification and partial characterization of the Mr 30,000 integral membrane-protein associated with the erythrocyte Rh(D) antigen. Journal Of Biological Chemistry 262: 17497-17503.
    • (1987) Journal Of Biological Chemistry , vol.262 , pp. 17497-17503
    • Agre, P.P.1    Saboori, A.M.2    Asimos, A.3    Smith, B.L.4
  • 18
    • 63449132403 scopus 로고    scopus 로고
    • Water channel proteins (later called aquaporins) and relatives: Past, present, and future
    • Benga G, (2009) Water channel proteins (later called aquaporins) and relatives: Past, present, and future. Iubmb Life 61: 112-133.
    • (2009) Iubmb Life , vol.61 , pp. 112-133
    • Benga, G.1
  • 19
    • 65649092165 scopus 로고    scopus 로고
    • Aquaporins are multifunctional water and solute transporters highly divergent in living organisms
    • Gomes D, Agasse A, Thiebaud P, Delrot S, Geros H, et al. (2009) Aquaporins are multifunctional water and solute transporters highly divergent in living organisms. Biochimica Et Biophysica Acta-biomembranes 1788: 1213-1228.
    • (2009) Biochimica Et Biophysica Acta-Biomembranes , vol.1788 , pp. 1213-1228
    • Gomes, D.1    Agasse, A.2    Thiebaud, P.3    Delrot, S.4    Geros, H.5
  • 21
  • 24
    • 0028919341 scopus 로고
    • Molecular-cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues
    • Raina S, Preston GM, Guggino WB, Agre P, (1995) Molecular-cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues. Journal Of Biological Chemistry 270: 1908-1912.
    • (1995) Journal Of Biological Chemistry , vol.270 , pp. 1908-1912
    • Raina, S.1    Preston, G.M.2    Guggino, W.B.3    Agre, P.4
  • 25
    • 0030922070 scopus 로고    scopus 로고
    • Water and glycerol permeabilities of aquaporins 1-5 and mip determined quantitatively by expression of epitope-tagged constructs in xenopus oocytes
    • Yang BX, Verkman AS, (1997) Water and glycerol permeabilities of aquaporins 1-5 and mip determined quantitatively by expression of epitope-tagged constructs in xenopus oocytes. Journal Of Biological Chemistry 272: 16140-16146.
    • (1997) Journal Of Biological Chemistry , vol.272 , pp. 16140-16146
    • Yang, B.X.1    Verkman, A.S.2
  • 29
    • 0031783914 scopus 로고    scopus 로고
    • Localization and expression of aqp5 in cornea, serous salivary glands, and pulmonary epithelial cells
    • Funaki H, Yamamoto T, Koyama Y, Kondo D, Yaoita E, et al. (1998) Localization and expression of aqp5 in cornea, serous salivary glands, and pulmonary epithelial cells. Am J Physiol 275: C1151-7.
    • (1998) Am J Physiol , vol.275
    • Funaki, H.1    Yamamoto, T.2    Koyama, Y.3    Kondo, D.4    Yaoita, E.5
  • 31
    • 0033009356 scopus 로고    scopus 로고
    • Aquaporin-5 (aqp5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation
    • Matsuzaki T, Suzuki T, Koyama H, Tanaka S, Takata K, (1999) Aquaporin-5 (aqp5), a water channel protein, in the rat salivary and lacrimal glands: immunolocalization and effect of secretory stimulation. Cell and Tissue Research 295: 513-521.
    • (1999) Cell and Tissue Research , vol.295 , pp. 513-521
    • Matsuzaki, T.1    Suzuki, T.2    Koyama, H.3    Tanaka, S.4    Takata, K.5
  • 37
    • 0038460939 scopus 로고    scopus 로고
    • Distribution of aquaporin water channels aqp1 and aqp5 in the ductal system of the human pancreas
    • Burghardt B, Elkjaer ML, Kwon TH, Racz GZ, Varga G, et al. (2003) Distribution of aquaporin water channels aqp1 and aqp5 in the ductal system of the human pancreas. Gut 52: 1008-1016.
    • (2003) Gut , vol.52 , pp. 1008-1016
    • Burghardt, B.1    Elkjaer, M.L.2    Kwon, T.H.3    Racz, G.Z.4    Varga, G.5
  • 38
    • 26844545317 scopus 로고    scopus 로고
    • Identification of aqp5 in lipid rafts and its translocation to apical membranes by activation of m-3 machrs in interlobular ducts of rat parotid gland
    • Ishikawa Y, Yuan Z, Inoue N, Skowronski MT, Nakae Y, et al. (2005) Identification of aqp5 in lipid rafts and its translocation to apical membranes by activation of m-3 machrs in interlobular ducts of rat parotid gland. American Journal of Physiology-cell Physiology 289: C1303-C1311.
    • (2005) American Journal of Physiology-Cell Physiology , vol.289
    • Ishikawa, Y.1    Yuan, Z.2    Inoue, N.3    Skowronski, M.T.4    Nakae, Y.5
  • 39
    • 84860857809 scopus 로고    scopus 로고
    • Spatial expression of aquaporin 5 in mammalian cornea and lens, and regulation of its localization by phosphokinase a
    • Kumari SS, Varadaraj M, Yerramilli VS, Menon AG, Varadaraj K, (2012) Spatial expression of aquaporin 5 in mammalian cornea and lens, and regulation of its localization by phosphokinase a. Molecular Vision 18: 957-967.
    • (2012) Molecular Vision , vol.18 , pp. 957-967
    • Kumari, S.S.1    Varadaraj, M.2    Yerramilli, V.S.3    Menon, A.G.4    Varadaraj, K.5
  • 40
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and glpf
    • de Groot BL, Grubmüller H, (2001) Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and glpf. Science 294: 2353-2357.
    • (2001) Science , vol.294 , pp. 2353-2357
    • de Groot, B.L.1    Grubmüller, H.2
  • 41
    • 0242269040 scopus 로고    scopus 로고
    • Electrostatic tuning of permeation and selectivity in aquaporin water channels
    • Jensen MØ, Tajkhorshid E, Schulten K, (2003) Electrostatic tuning of permeation and selectivity in aquaporin water channels. Biophys J 85: 2884-2899.
    • (2003) Biophys J , vol.85 , pp. 2884-2899
    • Jensen, M.Ø.1    Tajkhorshid, E.2    Schulten, K.3
  • 44
    • 34248233008 scopus 로고    scopus 로고
    • Plant aquaporins: Novel functions and regulation properties
    • Maurel C, (2007) Plant aquaporins: Novel functions and regulation properties. Febs Letters 581: 2227-2236.
    • (2007) Febs Letters , vol.581 , pp. 2227-2236
    • Maurel, C.1
  • 46
    • 84857692588 scopus 로고    scopus 로고
    • Functional characterization of a novel aquaporin from dictyostelium discoideum amoebae implies a unique gating mechanism
    • von Bulow J, Muller-Lucks A, Kai L, Bernhard F, Beitz E, (2012) Functional characterization of a novel aquaporin from dictyostelium discoideum amoebae implies a unique gating mechanism. Journal of Biological Chemistry 287: 7487-7494.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 7487-7494
    • von Bulow, J.1    Muller-Lucks, A.2    Kai, L.3    Bernhard, F.4    Beitz, E.5
  • 47
    • 0032029335 scopus 로고    scopus 로고
    • Water transport activity of the plasma membrane aquaporin pm28a is regulated by phosphorylation
    • Johansson I, Karlsson M, Shukla VK, Chrispeels MJ, Larsson C, et al. (1998) Water transport activity of the plasma membrane aquaporin pm28a is regulated by phosphorylation. Plant Cell 10: 451-459.
    • (1998) Plant Cell , vol.10 , pp. 451-459
    • Johansson, I.1    Karlsson, M.2    Shukla, V.K.3    Chrispeels, M.J.4    Larsson, C.5
  • 48
    • 0141484616 scopus 로고    scopus 로고
    • Cytosolic ph regulates root water transport during anoxic stress through gating of aquaporins
    • Tournaire-Roux C, Sutka M, Javot H, Gout E, Gerbeau P, et al. (2003) Cytosolic ph regulates root water transport during anoxic stress through gating of aquaporins. Nature 425: 393-397.
    • (2003) Nature , vol.425 , pp. 393-397
    • Tournaire-Roux, C.1    Sutka, M.2    Javot, H.3    Gout, E.4    Gerbeau, P.5
  • 49
    • 58149156187 scopus 로고    scopus 로고
    • Structure-function analysis of plant aquaporin atpip2;1 gating by divalent cations and protons
    • Verdoucq L, Grondin A, Maurel C, (2008) Structure-function analysis of plant aquaporin atpip2;1 gating by divalent cations and protons. Biochemical Journal 415: 409-416.
    • (2008) Biochemical Journal , vol.415 , pp. 409-416
    • Verdoucq, L.1    Grondin, A.2    Maurel, C.3
  • 53
    • 33746730535 scopus 로고    scopus 로고
    • Does co2 permeate through aquaporin-1?
    • Hub JS, de Groot BL, (2006) Does co2 permeate through aquaporin-1? Biophysical Journal 91: 842-848.
    • (2006) Biophysical Journal , vol.91 , pp. 842-848
    • Hub, J.S.1    de Groot, B.L.2
  • 58
    • 84986440341 scopus 로고
    • Settle - an analytical version of the shake and rattle algorithm for rigid water models
    • Miyamoto S, Kollman PA, (1992) Settle- an analytical version of the shake and rattle algorithm for rigid water models. Journal of Computational Chemistry 13: 952-962.
    • (1992) Journal of Computational Chemistry , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 59
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen T, Sliz P, Kistler J, Cheng Y, Walz T, (2004) Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429: 193-197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 62
    • 1542747445 scopus 로고    scopus 로고
    • Single-file transport of water molecules through a carbon nanotube
    • Berezhkovskii A, Hummer G, (2002) Single-file transport of water molecules through a carbon nanotube. Phys Rev Lett 89: 064503.
    • (2002) Phys Rev Lett , vol.89 , pp. 064503
    • Berezhkovskii, A.1    Hummer, G.2
  • 63
    • 0347946756 scopus 로고    scopus 로고
    • Theory and simulation of water permeation in aquaporin-1
    • Zhu FQ, Tajkhorshid E, Schulten K, (2004) Theory and simulation of water permeation in aquaporin-1. Biophys J 86: 50-57.
    • (2004) Biophys J , vol.86 , pp. 50-57
    • Zhu, F.Q.1    Tajkhorshid, E.2    Schulten, K.3
  • 64
    • 42749105522 scopus 로고    scopus 로고
    • Collective diffusion model for water permeation through microscopic channels
    • Zhu FQ, Tajkhorshid E, Schulten K, (2004) Collective diffusion model for water permeation through microscopic channels. Phys Rev Lett 93: 224501.
    • (2004) Phys Rev Lett , vol.93 , pp. 224501
    • Zhu, F.Q.1    Tajkhorshid, E.2    Schulten, K.3
  • 68
    • 51749095497 scopus 로고    scopus 로고
    • Maize plasma membrane aquaporins belonging to the pip1 and pip2 subgroups are in vivo phosphorylated
    • Van Wilder V, Miecielica U, Degand H, Derua R, Waelkens E, et al. (2008) Maize plasma membrane aquaporins belonging to the pip1 and pip2 subgroups are in vivo phosphorylated. Plant and Cell Physiology 49: 1364-1377.
    • (2008) Plant and Cell Physiology , vol.49 , pp. 1364-1377
    • Van Wilder, V.1    Miecielica, U.2    Degand, H.3    Derua, R.4    Waelkens, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.