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Volumn 73, Issue 1, 2014, Pages 4-15

Conformational changes in dopamine transporter intracellular regions upon cocaine binding and dopamine translocation

Author keywords

Cocaine binding; Cysteine accessibility; Dopamine transport; Dopamine transporter (DAT); Molecular dynamics simulations

Indexed keywords

AMMONIUM DERIVATIVE; COCAINE; CYSTEINE; DOPAMINE; DOPAMINE TRANSPORTER; METHANETHIOSULFONATE ETHYL AMMONIUM; PHENYLALANINE; SERINE; SOLVENT; THIOL REAGENT; TYRAMINE; UNCLASSIFIED DRUG; ZINC; 2-CARBOMETHOXY-3-(3',4'-DICHLOROPHENYL)TROPANE; DOPAMINE UPTAKE INHIBITOR; TROPANE DERIVATIVE;

EID: 84902543559     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2014.02.003     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0032104581 scopus 로고    scopus 로고
    • Neurotransmitter transporters as molecular targets for addictive drugs
    • S.G. Amara, and M.S. Sonders Neurotransmitter transporters as molecular targets for addictive drugs Drug Alcohol Depend. 51 1998 87 96
    • (1998) Drug Alcohol Depend. , vol.51 , pp. 87-96
    • Amara, S.G.1    Sonders, M.S.2
  • 2
    • 33751194447 scopus 로고    scopus 로고
    • A comprehensive structure-based alignment of prokaryotic and eukaryotic neurotransmitter/Na+ symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function
    • T. Beuming, L. Shi, J.A. Javitch, and H. Weinstein A comprehensive structure-based alignment of prokaryotic and eukaryotic neurotransmitter/Na+ symporters (NSS) aids in the use of the LeuT structure to probe NSS structure and function Mol. Pharmacol. 70 2006 1630 1642
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1630-1642
    • Beuming, T.1    Shi, L.2    Javitch, J.A.3    Weinstein, H.4
  • 5
    • 0032535582 scopus 로고    scopus 로고
    • Cocaine acts as an apparent competitive inhibitor at the outward-facing conformation of the human norepinephrine transporter: Kinetic analysis of inward and outward transport
    • N. Chen, and J.B. Justice Jr. Cocaine acts as an apparent competitive inhibitor at the outward-facing conformation of the human norepinephrine transporter: kinetic analysis of inward and outward transport J. Neurosci. 18 1998 10257 10268
    • (1998) J. Neurosci. , vol.18 , pp. 10257-10268
    • Chen, N.1    Justice, Jr.J.B.2
  • 6
    • 0030692041 scopus 로고    scopus 로고
    • The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding
    • J.-G. Chen, A. Sachpatzidis, and G. Rudnick The third transmembrane domain of the serotonin transporter contains residues associated with substrate and cocaine binding J. Biol. Chem. 272 1997 28321 28327
    • (1997) J. Biol. Chem. , vol.272 , pp. 28321-28327
    • Chen, J.-G.1    Sachpatzidis, A.2    Rudnick, G.3
  • 7
    • 0034695678 scopus 로고    scopus 로고
    • Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter
    • N. Chen, J.V. Ferrer, J.A. Javitch, and J.B. Justice Transport-dependent accessibility of a cytoplasmic loop cysteine in the human dopamine transporter J. Biol. Chem. 275 2000 1608 1614
    • (2000) J. Biol. Chem. , vol.275 , pp. 1608-1614
    • Chen, N.1    Ferrer, J.V.2    Javitch, J.A.3    Justice, J.B.4
  • 8
    • 1242317021 scopus 로고    scopus 로고
    • Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding
    • N. Chen, J. Rickey, J.L. Berfield, and M.E.A. Reith Aspartate 345 of the dopamine transporter is critical for conformational changes in substrate translocation and cocaine binding J. Biol. Chem. 279 2004 5508 5519
    • (2004) J. Biol. Chem. , vol.279 , pp. 5508-5519
    • Chen, N.1    Rickey, J.2    Berfield, J.L.3    Reith, M.E.A.4
  • 9
    • 84881430324 scopus 로고    scopus 로고
    • Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT
    • Mary.H. Cheng, and I. Bahar Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT Biophys. J. 105 2013 630 639
    • (2013) Biophys. J. , vol.105 , pp. 630-639
    • Cheng, Mary.H.1    Bahar, I.2
  • 10
    • 0030930379 scopus 로고    scopus 로고
    • Metabolism of catecholamines by catechol-O-methyltransferase in cells expressing recombinant catecholamine transporters
    • A.J. Eshleman, E. Stewart, A.K. Evenson, J.N. Mason, R.D. Blakely, A. Janowsky, and K.A. Neve Metabolism of catecholamines by catechol-O- methyltransferase in cells expressing recombinant catecholamine transporters J. Neurochem. 69 1997 1459 1466
    • (1997) J. Neurochem. , vol.69 , pp. 1459-1466
    • Eshleman, A.J.1    Stewart, E.2    Evenson, A.K.3    Mason, J.N.4    Blakely, R.D.5    Janowsky, A.6    Neve, K.A.7
  • 11
    • 0032482945 scopus 로고    scopus 로고
    • Cocaine alters the accessibility of endogenous cysteines in putative extracellular and intracellular loops of the human dopamine transporter
    • J.V. Ferrer, and J.A. Javitch Cocaine alters the accessibility of endogenous cysteines in putative extracellular and intracellular loops of the human dopamine transporter Proc. Natl. Acad. Sci. USA 95 1998 9238 9243
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9238-9243
    • Ferrer, J.V.1    Javitch, J.A.2
  • 12
    • 33745714411 scopus 로고    scopus 로고
    • On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins
    • L.R. Forrest, C.L. Tang, and B. Honig On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins Biophys. J. 91 2006 508 517
    • (2006) Biophys. J. , vol.91 , pp. 508-517
    • Forrest, L.R.1    Tang, C.L.2    Honig, B.3
  • 14
    • 0028229855 scopus 로고
    • Stable expression of biogenic amine transporters reveals differences in inhibitor sensitivity, kinetics, and ion dependence
    • H. Gu, S.C. Wall, and G. Rudnick Stable expression of biogenic amine transporters reveals differences in inhibitor sensitivity, kinetics, and ion dependence J. Biol. Chem. 269 1994 7124 7130
    • (1994) J. Biol. Chem. , vol.269 , pp. 7124-7130
    • Gu, H.1    Wall, S.C.2    Rudnick, G.3
  • 15
    • 0035964192 scopus 로고    scopus 로고
    • Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment
    • H. Hastrup, A. Karlin, and J.A. Javitch Symmetrical dimer of the human dopamine transporter revealed by cross-linking Cys-306 at the extracellular end of the sixth transmembrane segment Proc. Natl. Acad. Sci. USA 98 2001 10055 10060
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10055-10060
    • Hastrup, H.1    Karlin, A.2    Javitch, J.A.3
  • 16
    • 33645783040 scopus 로고    scopus 로고
    • Probing a model of a GPCR/ligand complex in an explicit membrane environment: The human cholecystokinin-1 receptor
    • J. Henin, B. Maigret, M. Tarek, C. Escrieut, D. Fourmy, and C. Chipot Probing a model of a GPCR/ligand complex in an explicit membrane environment: the human cholecystokinin-1 receptor Biophys. J. 90 2006 1232 1240
    • (2006) Biophys. J. , vol.90 , pp. 1232-1240
    • Henin, J.1    Maigret, B.2    Tarek, M.3    Escrieut, C.4    Fourmy, D.5    Chipot, C.6
  • 17
    • 0141844649 scopus 로고    scopus 로고
    • Serotonin and cocaine-sensitive inactivation of human serotonin transporters by methanethiosulfonates targeted to transmembrane domain i
    • L.K. Henry, E.M. Adkins, Q. Han, and R.D. Blakely Serotonin and cocaine-sensitive inactivation of human serotonin transporters by methanethiosulfonates targeted to transmembrane domain I J. Biol. Chem. 278 2003 37052 37063
    • (2003) J. Biol. Chem. , vol.278 , pp. 37052-37063
    • Henry, L.K.1    Adkins, E.M.2    Han, Q.3    Blakely, R.D.4
  • 18
    • 72449145780 scopus 로고    scopus 로고
    • Mechanism for cocaine blocking the transport of dopamine: Insights from molecular modeling and dynamics simulations
    • X. Huang, H.H. Gu, and C.-G. Zhan Mechanism for cocaine blocking the transport of dopamine: insights from molecular modeling and dynamics simulations J. Phys. Chem. B 113 2009 15057 15066
    • (2009) J. Phys. Chem. B , vol.113 , pp. 15057-15066
    • Huang, X.1    Gu, H.H.2    Zhan, C.-G.3
  • 19
  • 20
    • 44849091207 scopus 로고    scopus 로고
    • Sodium-coupled neurotransmitter transporters
    • B.I. Kanner, and E. Zomot Sodium-coupled neurotransmitter transporters Chem. Rev. 108 2008 1654 1668
    • (2008) Chem. Rev. , vol.108 , pp. 1654-1668
    • Kanner, B.I.1    Zomot, E.2
  • 21
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • A. Karlin, and M.H. Akabas Substituted-cysteine accessibility method Methods Enzymol. 293 1998 123 145
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 22
    • 59849093622 scopus 로고    scopus 로고
    • Structural determinants of species-selective substrate recognition in human and drosophila serotonin transporters revealed through computational docking studies
    • K.W. Kaufmann, E.S. Dawson, L.K. Henry, J.R. Field, R.D. Blakely, and J. Meiler Structural determinants of species-selective substrate recognition in human and drosophila serotonin transporters revealed through computational docking studies Proteins 74 2009 630 642
    • (2009) Proteins , vol.74 , pp. 630-642
    • Kaufmann, K.W.1    Dawson, E.S.2    Henry, L.K.3    Field, J.R.4    Blakely, R.D.5    Meiler, J.6
  • 23
    • 47749083479 scopus 로고    scopus 로고
    • An intracellular interaction network regulates conformational transitions in the dopamine transporter
    • J. Kniazeff, L. Shi, C.J. Loland, J.A. Javitch, H. Weinstein, and U. Gether An intracellular interaction network regulates conformational transitions in the dopamine transporter J. Biol. Chem. 283 2008 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    Gether, U.6
  • 24
    • 0026507628 scopus 로고
    • Drugs of abuse: Anatomy, pharmacology and function of reward pathways
    • G.F. Koob Drugs of abuse: anatomy, pharmacology and function of reward pathways Trends Pharmacol. Sci. 13 1992 177 184
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 177-184
    • Koob, G.F.1
  • 25
    • 27844506567 scopus 로고    scopus 로고
    • Identification and selective inhibition of the channel mode of the neuronal GABA transporter 1
    • S. Krause, and W. Schwarz Identification and selective inhibition of the channel mode of the neuronal GABA transporter 1 Mol. Pharmacol. 68 2005 1728 1735
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1728-1735
    • Krause, S.1    Schwarz, W.2
  • 26
    • 84856225222 scopus 로고    scopus 로고
    • X-ray structures of LeuT in substrate-free outward-open and apo inward-open states
    • H. Krishnamurthy, and E. Gouaux X-ray structures of LeuT in substrate-free outward-open and apo inward-open states Nature 481 2012 469 474
    • (2012) Nature , vol.481 , pp. 469-474
    • Krishnamurthy, H.1    Gouaux, E.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0033601168 scopus 로고    scopus 로고
    • Defining proximity relationships in the tertiary structure of the dopamine transporter
    • C.J. Loland, L. Norregaard, and U. Gether Defining proximity relationships in the tertiary structure of the dopamine transporter J. Biol. Chem. 274 1999 36928 36934
    • (1999) J. Biol. Chem. , vol.274 , pp. 36928-36934
    • Loland, C.J.1    Norregaard, L.2    Gether, U.3
  • 29
    • 0037022356 scopus 로고    scopus 로고
    • Generation of an activating Zn(2+) switch in the dopamine transporter: Mutation of an intracellular tyrosine constitutively alters the conformational equilibrium of the transport cycle
    • C.J. Loland, L. Norregaard, T. Litman, and U. Gether Generation of an activating Zn(2+) switch in the dopamine transporter: mutation of an intracellular tyrosine constitutively alters the conformational equilibrium of the transport cycle Proc. Natl. Acad. Sci. USA 99 2002 1683 1688
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1683-1688
    • Loland, C.J.1    Norregaard, L.2    Litman, T.3    Gether, U.4
  • 30
    • 0942276396 scopus 로고    scopus 로고
    • Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding
    • C.J. Loland, C. Granas, J.A. Javitch, and U. Gether Identification of intracellular residues in the dopamine transporter critical for regulation of transporter conformation and cocaine binding J. Biol. Chem. 279 2004 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
  • 31
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • S. Miller, A.M. Lesk, J. Janin, and C. Chothia The accessible surface area and stability of oligomeric proteins Nature 328 1987 834 836
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 33
    • 0032480011 scopus 로고    scopus 로고
    • Delineation of an endogenous zinc-binding site in the human dopamine transporter
    • L. Norregaard, D. Frederiksen, E.O. Nielsen, and U. Gether Delineation of an endogenous zinc-binding site in the human dopamine transporter EMBO J. 17 1998 4266 4273
    • (1998) EMBO J. , vol.17 , pp. 4266-4273
    • Norregaard, L.1    Frederiksen, D.2    Nielsen, E.O.3    Gether, U.4
  • 34
    • 84887404259 scopus 로고    scopus 로고
    • X-ray structure of dopamine transporter elucidates antidepressant mechanism
    • A. Penmatsa, K.H. Wang, and E. Gouaux X-ray structure of dopamine transporter elucidates antidepressant mechanism Nature 503 2013 85 90
    • (2013) Nature , vol.503 , pp. 85-90
    • Penmatsa, A.1    Wang, K.H.2    Gouaux, E.3
  • 35
    • 0031875263 scopus 로고    scopus 로고
    • Macrophage scavenger receptor confers an adherent phenotype to cells in culture
    • A.K. Robbins, and R.A. Horlick Macrophage scavenger receptor confers an adherent phenotype to cells in culture Biotechniques 25 1998 240 244
    • (1998) Biotechniques , vol.25 , pp. 240-244
    • Robbins, A.K.1    Horlick, R.A.2
  • 36
    • 0001951796 scopus 로고    scopus 로고
    • Mechanisms of biogenic amine neurotransmitter transporters
    • M.E. Reith, 2nd ed. Humana Press Inc. Totowa, New Jersey
    • G. Rudnick Mechanisms of biogenic amine neurotransmitter transporters M.E. Reith, Neurotransmitter transporters: structure, function, and regulation 2nd ed. 2002 Humana Press Inc. Totowa, New Jersey 25 52
    • (2002) Neurotransmitter Transporters: Structure, Function, and Regulation , pp. 25-52
    • Rudnick, G.1
  • 37
    • 34247233255 scopus 로고    scopus 로고
    • Serotonin transporters-structure and function
    • G. Rudnick Serotonin transporters-structure and function J. Membr. Biol. 213 2006 101 110
    • (2006) J. Membr. Biol. , vol.213 , pp. 101-110
    • Rudnick, G.1
  • 39
    • 79551598571 scopus 로고    scopus 로고
    • The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter
    • J. Shan, J.A. Javitch, L. Shi, and H. Weinstein The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter PLoS One 6 2011 e16350
    • (2011) PLoS One , vol.6 , pp. 16350
    • Shan, J.1    Javitch, J.A.2    Shi, L.3    Weinstein, H.4
  • 40
    • 44949086583 scopus 로고    scopus 로고
    • The mechanism of a neurotransmitter:sodium symporter-inward release of Na+ and substrate is triggered by substrate in a second binding site
    • L. Shi, M. Quick, Y. Zhao, H. Weinstein, and J.A. Javitch 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 2008 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
  • 41
    • 34548178234 scopus 로고    scopus 로고
    • Antidepressant binding site in a bacterial homologue of neurotransmitter transporters
    • S.K. Singh, A. Yamashita, and E. Gouaux Antidepressant binding site in a bacterial homologue of neurotransmitter transporters Nature 448 2007 952 956
    • (2007) Nature , vol.448 , pp. 952-956
    • Singh, S.K.1    Yamashita, A.2    Gouaux, E.3
  • 42
    • 58149233796 scopus 로고    scopus 로고
    • A competitive inhibitor traps LeuT in an open-to-out conformation
    • S.K. Singh, C.L. Piscitelli, A. Yamashita, and E. Gouaux A competitive inhibitor traps LeuT in an open-to-out conformation Science 322 2008 1655 1661
    • (2008) Science , vol.322 , pp. 1655-1661
    • Singh, S.K.1    Piscitelli, C.L.2    Yamashita, A.3    Gouaux, E.4
  • 43
    • 20444428381 scopus 로고    scopus 로고
    • How did the neurotransmitter cross the bilayer? A closer view
    • M.S. Sonders, M. Quick, and J.A. Javitch How did the neurotransmitter cross the bilayer? A closer view Curr. Opin. Neurobiol. 15 2005 296 304
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 296-304
    • Sonders, M.S.1    Quick, M.2    Javitch, J.A.3
  • 44
    • 0037264650 scopus 로고    scopus 로고
    • Plasma membrane monoamine transporters: Structure, regulation and function
    • G.E. Torres, R.R. Gainetdinov, and M.G. Caron Plasma membrane monoamine transporters: structure, regulation and function Nat. Rev. Neurosci. 4 2003 13 25
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 13-25
    • Torres, G.E.1    Gainetdinov, R.R.2    Caron, M.G.3
  • 45
    • 1642293724 scopus 로고    scopus 로고
    • Mechanism of action of methylphenidate: Insights from PET imaging studies
    • N.D. Volkow, J.S. Fowler, G. Wang, Y. Ding, and S.J. Gatley Mechanism of action of methylphenidate: insights from PET imaging studies J. Atten. Disord. 6 Suppl. 1 2002 S31 43
    • (2002) J. Atten. Disord. , vol.6 , Issue.SUPPL. 1 , pp. 31-43
    • Volkow, N.D.1    Fowler, J.S.2    Wang, G.3    Ding, Y.4    Gatley, S.J.5
  • 46
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters
    • A. Yamashita, S.K. Singh, T. Kawate, Y. Jin, and E. Gouaux Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters Nature 437 2005 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
  • 47
    • 33845966416 scopus 로고    scopus 로고
    • The cytoplasmic substrate permeation pathway of serotonin transporter
    • Y.-W. Zhang, and G. Rudnick The cytoplasmic substrate permeation pathway of serotonin transporter J. Biol. Chem. 281 2006 36213 36220
    • (2006) J. Biol. Chem. , vol.281 , pp. 36213-36220
    • Zhang, Y.-W.1    Rudnick, G.2
  • 48
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Y. Zhao, D. Terry, L. Shi, H. Weinstein, S.C. Blanchard, and J.A. Javitch Single-molecule dynamics of gating in a neurotransmitter transporter homologue Nature 465 2010 188 193
    • (2010) Nature , vol.465 , pp. 188-193
    • Zhao, Y.1    Terry, D.2    Shi, L.3    Weinstein, H.4    Blanchard, S.C.5    Javitch, J.A.6
  • 49
    • 79957935490 scopus 로고    scopus 로고
    • Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue
    • Y. Zhao, D.S. Terry, L. Shi, M. Quick, H. Weinstein, S.C. Blanchard, and J.A. Javitch Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue Nature 474 2011 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    Blanchard, S.C.6    Javitch, J.A.7
  • 50
    • 34548684744 scopus 로고    scopus 로고
    • LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake
    • Z. Zhou, J. Zhen, N.K. Karpowich, R.M. Goetz, C.J. Law, M.E.A. Reith, and D.-N. Wang LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake Science 317 2007 1390 1393
    • (2007) Science , vol.317 , pp. 1390-1393
    • Zhou, Z.1    Zhen, J.2    Karpowich, N.K.3    Goetz, R.M.4    Law, C.J.5    Reith, M.E.A.6    Wang, D.-N.7


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