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Volumn 10, Issue 10, 2014, Pages

Complete Mapping of Substrate Translocation Highlights the Role of LeuT N-terminal Segment in Regulating Transport Cycle

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; FACINGS; METAL IONS; MOLECULES; NEUROPHYSIOLOGY;

EID: 84908333081     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003879     Document Type: Article
Times cited : (54)

References (48)
  • 1
    • 66249098083 scopus 로고    scopus 로고
    • Unlocking the molecular secrets of sodium-coupled transporters
    • Krishnamurthy H, Piscitelli CL, Gouaux E, (2009) Unlocking the molecular secrets of sodium-coupled transporters. Nature 459: 347–355.
    • (2009) Nature , vol.459 , pp. 347-355
    • Krishnamurthy, H.1    Piscitelli, C.L.2    Gouaux, E.3
  • 2
    • 0032104581 scopus 로고    scopus 로고
    • Neurotransmitter transporters as molecular targets for addictive drugs
    • Amara SG, Sonders MS, (1998) Neurotransmitter transporters as molecular targets for addictive drugs. Drug Alcohol Depend 51: 87–96.
    • (1998) Drug Alcohol Depend , vol.51 , pp. 87-96
    • Amara, S.G.1    Sonders, M.S.2
  • 3
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky O, (1966) Simple allosteric model for membrane pumps. Nature 211: 969–970.
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 4
    • 84881430324 scopus 로고    scopus 로고
    • Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT
    • Cheng MH, Bahar I, (2013) Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT. Biophys J 105: 630–639.
    • (2013) Biophys J , vol.105 , pp. 630-639
    • Cheng, M.H.1    Bahar, I.2
  • 5
    • 24644470065 scopus 로고    scopus 로고
    • −-dependent neurotransmitter transporters
    • Yamashita A, Singh SK, Kawate T, Jin Y, Gouaux E, (2005) Crystal structure of a bacterial homologue of Na+/Cl−-dependent neurotransmitter transporters. Nature 437: 215–223.
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 6
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • Krishnamurthy H, Gouaux E, (2012) X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481: 469–474.
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 7
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • Singh SK, Piscitelli CL, Yamashita A, Gouaux E, (2008) A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322: 1655–1661.
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 9
    • 47749083479 scopus 로고    scopus 로고
    • An intracellular interaction network regulates conformational transitions in the dopamine transporter
    • Kniazeff J, Shi L, Loland CJ, Javitch JA, Weinstein H, et al. (2008) An intracellular interaction network regulates conformational transitions in the dopamine transporter. J Biol Chem 283: 17691–17701.
    • (2008) J Biol Chem , vol.283 , pp. 17691-17701
    • Kniazeff, J.1    Shi, L.2    Loland, C.J.3    Javitch, J.A.4    Weinstein, H.5
  • 10
    • 77951230460 scopus 로고    scopus 로고
    • The N terminus of monoamine transporters is a lever required for the action of amphetamines
    • Sucic S, Dallinger S, Zdrazil B, Weissensteiner R, Jorgensen TN, et al. (2010) The N terminus of monoamine transporters is a lever required for the action of amphetamines. J Biol Chem 285: 10924–10938.
    • (2010) J Biol Chem , vol.285 , pp. 10924-10938
    • Sucic, S.1    Dallinger, S.2    Zdrazil, B.3    Weissensteiner, R.4    Jorgensen, T.N.5
  • 11
    • 59649089311 scopus 로고    scopus 로고
    • Negative regulation of dopamine transporter endocytosis by membrane-proximal N-terminal residues
    • Sorkina T, Richards TL, Rao A, Zahniser NR, Sorkin A, (2009) Negative regulation of dopamine transporter endocytosis by membrane-proximal N-terminal residues. J Neurosci 29: 1361–1374.
    • (2009) J Neurosci , vol.29 , pp. 1361-1374
    • Sorkina, T.1    Richards, T.L.2    Rao, A.3    Zahniser, N.R.4    Sorkin, A.5
  • 12
    • 84875446139 scopus 로고    scopus 로고
    • Intracellular gating in an inward-facing state of aspartate transporter Glt(Ph) is regulated by the movements of the helical hairpin HP2
    • Zomot E, Bahar I, (2013) Intracellular gating in an inward-facing state of aspartate transporter Glt(Ph) is regulated by the movements of the helical hairpin HP2. J Biol Chem 288: 8231–8237.
    • (2013) J Biol Chem , vol.288 , pp. 8231-8237
    • Zomot, E.1    Bahar, I.2
  • 13
    • 78049427382 scopus 로고    scopus 로고
    • − dependent neurotransmitter transporter homologue
    • Shaikh SA, Tajkhorshid E, (2010) Modeling and dynamics of the inward-facing state of a Na+/Cl− dependent neurotransmitter transporter homologue. PLoS Comput Biol 6: e1000905.
    • (2010) PLoS Comput Biol , vol.6 , pp. e1000905
    • Shaikh, S.A.1    Tajkhorshid, E.2
  • 14
    • 84866376631 scopus 로고    scopus 로고
    • A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/gamma-butyrobetaine antiporter CaiT
    • Zomot E, Bahar I, (2012) A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/gamma-butyrobetaine antiporter CaiT. J Biol Chem 287: 31823–31832.
    • (2012) J Biol Chem , vol.287 , pp. 31823-31832
    • Zomot, E.1    Bahar, I.2
  • 15
    • 79957625386 scopus 로고    scopus 로고
    • Protonation of glutamate 208 induces the release of agmatine in an outward-facing conformation of an arginine/agmatine antiporter
    • Zomot E, Bahar I, (2011) Protonation of glutamate 208 induces the release of agmatine in an outward-facing conformation of an arginine/agmatine antiporter. J Biol Chem 286: 19693–19701.
    • (2011) J Biol Chem , vol.286 , pp. 19693-19701
    • Zomot, E.1    Bahar, I.2
  • 16
    • 77952481518 scopus 로고    scopus 로고
    • The sodium/galactose symporter crystal structure is a dynamic, not so occluded state
    • Zomot E, Bahar I, (2010) The sodium/galactose symporter crystal structure is a dynamic, not so occluded state. Mol Biosyst 6: 1040–1046.
    • (2010) Mol Biosyst , vol.6 , pp. 1040-1046
    • Zomot, E.1    Bahar, I.2
  • 18
    • 79952811744 scopus 로고    scopus 로고
    • The role of local hydration and hydrogen-bonding dynamics in ion and solute release from ion-coupled secondary transporters
    • Zhao C, Noskov SY, (2011) The role of local hydration and hydrogen-bonding dynamics in ion and solute release from ion-coupled secondary transporters. Biochemistry 50: 1848–1856.
    • (2011) Biochemistry , vol.50 , pp. 1848-1856
    • Zhao, C.1    Noskov, S.Y.2
  • 19
    • 84863476382 scopus 로고    scopus 로고
    • LeuT conformational sampling utilizing accelerated molecular dynamics and principal component analysis
    • Thomas JR, Gedeon PC, Grant BJ, Madura JD, (2012) LeuT conformational sampling utilizing accelerated molecular dynamics and principal component analysis. Biophys J 103: L1–3.
    • (2012) Biophys J , vol.103 , pp. L1-3
    • Thomas, J.R.1    Gedeon, P.C.2    Grant, B.J.3    Madura, J.D.4
  • 20
    • 78650306568 scopus 로고    scopus 로고
    • The mechanism of sodium and substrate release from the binding pocket of vSGLT
    • Watanabe A, Choe S, Chaptal V, Rosenberg JM, Wright EM, et al. (2010) The mechanism of sodium and substrate release from the binding pocket of vSGLT. Nature 468: 988–991.
    • (2010) Nature , vol.468 , pp. 988-991
    • Watanabe, A.1    Choe, S.2    Chaptal, V.3    Rosenberg, J.M.4    Wright, E.M.5
  • 21
    • 84873845174 scopus 로고    scopus 로고
    • Visualizing functional motions of membrane transporters with molecular dynamics simulations
    • Shaikh SA, Li J, Enkavi G, Wen PC, Huang Z, et al. (2013) Visualizing functional motions of membrane transporters with molecular dynamics simulations. Biochemistry 52: 569–587.
    • (2013) Biochemistry , vol.52 , pp. 569-587
    • Shaikh, S.A.1    Li, J.2    Enkavi, G.3    Wen, P.C.4    Huang, Z.5
  • 22
    • 3142716857 scopus 로고    scopus 로고
    • Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules
    • Hamelberg D, Mongan J, McCammon J, (2004) Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules. J Chem Phys 120: 11919–11929.
    • (2004) J Chem Phys , vol.120 , pp. 11919-11929
    • Hamelberg, D.1    Mongan, J.2    McCammon, J.3
  • 23
    • 85135501159 scopus 로고    scopus 로고
    • Das A, Gur M, Cheng MH, Jo S, Bahar I, et al. (2014) Exploring the conformational transitions of biomolecular systems using a simple two-state anisotropic network model. PLoS Comput Biol in press.
  • 24
    • 84867092080 scopus 로고    scopus 로고
    • Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP
    • Perez C, Koshy C, Yildiz O, Ziegler C, (2012) Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP. Nature 490: 126–130.
    • (2012) Nature , vol.490 , pp. 126-130
    • Perez, C.1    Koshy, C.2    Yildiz, O.3    Ziegler, C.4
  • 25
    • 77951585158 scopus 로고    scopus 로고
    • Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1
    • Shimamura T, Weyand S, Beckstein O, Rutherford NG, Hadden JM, et al. (2010) Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1. Science 328: 470–473.
    • (2010) Science , vol.328 , pp. 470-473
    • Shimamura, T.1    Weyand, S.2    Beckstein, O.3    Rutherford, N.G.4    Hadden, J.M.5
  • 26
    • 84877317987 scopus 로고    scopus 로고
    • Transient formation of water-conducting states in membrane transporters
    • Li J, Shaikh SA, Enkavi G, Wen PC, Huang Z, et al. (2013) Transient formation of water-conducting states in membrane transporters. Proc Natl Acad Sci U S A 110: 7696–7701.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7696-7701
    • Li, J.1    Shaikh, S.A.2    Enkavi, G.3    Wen, P.C.4    Huang, Z.5
  • 27
    • 44949086583 scopus 로고    scopus 로고
    • + and substrate is triggered by substrate in a second binding site
    • Shi L, Quick M, Zhao Y, Weinstein H, Javitch JA, (2008) The mechanism of a neurotransmitter:sodium symporter–inward release of Na+ and substrate is triggered by substrate in a second binding site. Mol Cell 30: 667–677.
    • (2008) Mol Cell , vol.30 , pp. 667-677
    • Shi, L.1    Quick, M.2    Zhao, Y.3    Weinstein, H.4    Javitch, J.A.5
  • 28
    • 79957935490 scopus 로고    scopus 로고
    • +-coupled neurotransmitter transporter homologue
    • Zhao Y, Terry DS, Shi L, Quick M, Weinstein H, et al. (2011) Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue. Nature 474: 109–113.
    • (2011) Nature , vol.474 , pp. 109-113
    • Zhao, Y.1    Terry, D.S.2    Shi, L.3    Quick, M.4    Weinstein, H.5
  • 29
    • 65249169367 scopus 로고    scopus 로고
    • Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation
    • Quick M, Winther AM, Shi L, Nissen P, Weinstein H, et al. (2009) Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation. Proc Natl Acad Sci U S A 106: 5563–5568.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5563-5568
    • Quick, M.1    Winther, A.M.2    Shi, L.3    Nissen, P.4    Weinstein, H.5
  • 31
    • 48749106109 scopus 로고    scopus 로고
    • +/sugar symport
    • Faham S, Watanabe A, Besserer GM, Cascio D, Specht A, et al. (2008) The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science 321: 810–814.
    • (2008) Science , vol.321 , pp. 810-814
    • Faham, S.1    Watanabe, A.2    Besserer, G.M.3    Cascio, D.4    Specht, A.5
  • 32
    • 0034602317 scopus 로고    scopus 로고
    • −)-coupled gamma-aminobutyric acid transporter from rat brain, impairs net flux but not exchange
    • Bennett ER, Su H, Kanner BI, (2000) Mutation of arginine 44 of GAT-1, a (Na+ + Cl−)-coupled gamma-aminobutyric acid transporter from rat brain, impairs net flux but not exchange. J Biol Chem 275: 34106–34113.
    • (2000) J Biol Chem , vol.275 , pp. 34106-34113
    • Bennett, E.R.1    Su, H.2    Kanner, B.I.3
  • 33
    • 0942276396 scopus 로고    scopus 로고
    • Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding
    • Loland CJ, Granas C, Javitch JA, Gether U, (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
  • 35
    • 0346882663 scopus 로고    scopus 로고
    • ModLoop: automated modeling of loops in protein structures
    • Fiser A, Sali A, (2003) ModLoop: automated modeling of loops in protein structures. Bioinformatics 19: 2500–2501.
    • (2003) Bioinformatics , vol.19 , pp. 2500-2501
    • Fiser, A.1    Sali, A.2
  • 37
    • 34547809547 scopus 로고
    • A Unified formulation of the constant-temperature molecular-dynamics methods
    • Nosé S, (1984) A Unified formulation of the constant-temperature molecular-dynamics methods. J Chem Phys 81: 511–519.
    • (1984) J Chem Phys , vol.81 , pp. 511-519
    • Nosé, S.1
  • 38
    • 0001538909 scopus 로고
    • Canonical dynamics: equilibrium phase-space distributions
    • Hoover W, (1985) Canonical dynamics: equilibrium phase-space distributions. Phys Rev A 31: 1695.
    • (1985) Phys Rev A , vol.31 , pp. 1695
    • Hoover, W.1
  • 39
    • 77955477744 scopus 로고    scopus 로고
    • Functional rotation of the transporter AcrB: insights into drug extrusion from simulations
    • Schulz R, Vargiu AV, Collu F, Kleinekathofer U, Ruggerone P, (2010) Functional rotation of the transporter AcrB: insights into drug extrusion from simulations. PLoS Comput Biol 6: e1000806.
    • (2010) PLoS Comput Biol , vol.6 , pp. e1000806
    • Schulz, R.1    Vargiu, A.V.2    Collu, F.3    Kleinekathofer, U.4    Ruggerone, P.5
  • 40
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell AD, Bashford D, Bellott M, Dunbrack RL, Evanseck JD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102: 3586–3616.
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • Mackerell, A.D.1    Bashford, D.2    Bellott, M.3    Dunbrack, R.L.4    Evanseck, J.D.5
  • 41
    • 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, JrFeig M, Brooks CL, 3rd (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
  • 42
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM All-Atom Additive Force Field for Lipids: Validation on Six Lipid Types
    • Klauda JB, Venable RM, Freites JA, O'Connor JW, Tobias DJ, 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
    • Klauda, J.B.1    Venable, R.M.2    Freites, J.A.3    O'Connor, J.W.4
  • 44
    • 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
  • 45
    • 79957788878 scopus 로고    scopus 로고
    • ProDy: protein dynamics inferred from theory and experiments
    • Bakan A, Meireles LM, Bahar I, (2011) ProDy: protein dynamics inferred from theory and experiments. Bioinformatics 27: 1575–1577.
    • (2011) Bioinformatics , vol.27 , pp. 1575-1577
    • Bakan, A.1    Meireles, L.M.2    Bahar, I.3
  • 46
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: systematic evaluation and a new web interface
    • Eyal E, Yang LW, Bahar I, (2006) Anisotropic network model: systematic evaluation and a new web interface. Bioinformatics 22: 2619–2627.
    • (2006) Bioinformatics , vol.22 , pp. 2619-2627
    • Eyal, E.1    Yang, L.W.2    Bahar, I.3
  • 48
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: a program for the analysis of the pore dimensions of ion channel structural models
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MS, (1996) HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph 14: 354–360.
    • (1996) J Mol Graph , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5


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