메뉴 건너뛰기




Volumn 502, Issue 7469, 2013, Pages 119-123

Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters

Author keywords

[No Author keywords available]

Indexed keywords

EXCITATORY AMINO ACID TRANSPORTER;

EID: 84885606528     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12538     Document Type: Article
Times cited : (108)

References (28)
  • 1
    • 44849091207 scopus 로고    scopus 로고
    • Sodium-coupled neurotransmitter transporters
    • Kanner, B. I. & Zomot, E. Sodium-coupled neurotransmitter transporters. Chem. Rev. 108, 1654-1668 (2008).
    • (2008) Chem. Rev. , vol.108 , pp. 1654-1668
    • Kanner, B.I.1    Zomot, E.2
  • 2
    • 77951680965 scopus 로고    scopus 로고
    • Na1: Aspartate coupling stoichiometry in the glutamate transporter homologue GltPh
    • Groeneveld, M. & Slotboom, D. J. Na1:aspartate coupling stoichiometry in the glutamate transporter homologue GltPh. Biochemistry 49, 3511-3513 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3511-3513
    • Groeneveld, M.1    Slotboom, D.J.2
  • 3
    • 72449164409 scopus 로고    scopus 로고
    • Transportmechanismof a bacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C. & Boudker, O. Transportmechanismof a bacterial homologue of glutamate transporters. Nature 462, 880-885 (2009).
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 4
    • 67650526059 scopus 로고    scopus 로고
    • Functional characterization of a Na1-dependent aspartate transporter from Pyrococcus horikoshii
    • Ryan, R. M., Compton, E. L. & Mindell, J. A. Functional characterization of a Na1-dependent aspartate transporter from Pyrococcus horikoshii. J. Biol. Chem. 284, 17540-17548 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 17540-17548
    • Ryan, R.M.1    Compton, E.L.2    Mindell, J.A.3
  • 5
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue fromPyrococcus horikoshii
    • Yernool, D. et al. Structure of a glutamate transporter homologue fromPyrococcus horikoshii. Nature 431, 811-818 (2004).
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1
  • 6
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O. et al. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445, 387-393 (2007).
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1
  • 7
    • 34247648737 scopus 로고    scopus 로고
    • The uncoupled chloride conductance of a bacterial glutamate transporter homolog
    • Ryan, R. M. & Mindell, J. A. The uncoupled chloride conductance of a bacterial glutamate transporter homolog. Nature Struct. Mol. Biol. 14, 365-371 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 365-371
    • Ryan, R.M.1    Mindell, J.A.2
  • 8
    • 84857992685 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog
    • Verdon, G. & Boudker, O. Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nature Struct. Mol. Biol. 19, 355-357 (2012).
    • (2012) Nature Struct. Mol. Biol. , vol.19 , pp. 355-357
    • Verdon, G.1    Boudker, O.2
  • 9
    • 84873571301 scopus 로고    scopus 로고
    • Conformational ensemble of the sodium-coupled aspartate transporter
    • Georgieva, E. R. et al. Conformational ensemble of the sodium-coupled aspartate transporter. Nature Struct. Mol. Biol. 20, 215-221 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 215-221
    • Georgieva, E.R.1
  • 10
    • 84873570870 scopus 로고    scopus 로고
    • Conformational heterogeneity of the aspartate transporter GltPh
    • Hänelt, I. et al. Conformational heterogeneity of the aspartate transporter GltPh. Nature Struct. Mol. Biol. 20, 210-214 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 210-214
    • Hänelt, I.1
  • 11
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo, C. et al. Advances in single-molecule fluorescence methods for molecular biology. Annu. Rev. Biochem. 77, 51-76 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 51-76
    • Joo, C.1
  • 12
    • 84855476209 scopus 로고    scopus 로고
    • Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy
    • Verhalen, B. et al. Dynamic ligand-induced conformational rearrangements in P-glycoprotein as probed by fluorescence resonance energy transfer spectroscopy. J. Biol. Chem. 287, 1112-1127 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 1112-1127
    • Verhalen, B.1
  • 13
    • 79957935490 scopus 로고    scopus 로고
    • Substrate-modulated gating dynamics in a Na1-coupled neurotransmitter transporter homologue
    • Zhao, Y. et al. Substrate-modulated gating dynamics in a Na1-coupled neurotransmitter transporter homologue. Nature 474, 109-113 (2011).
    • (2011) Nature , vol.474 , pp. 109-113
    • Zhao, Y.1
  • 14
    • 77952402284 scopus 로고    scopus 로고
    • Single-molecule dynamics of gating in a neurotransmitter transporter homologue
    • Zhao, Y. et al. Single-molecule dynamics of gating in a neurotransmitter transporter homologue. Nature 465, 188-193 (2010).
    • (2010) Nature , vol.465 , pp. 188-193
    • Zhao, Y.1
  • 15
    • 84885669136 scopus 로고    scopus 로고
    • Transport dynamics in a glutamate transporter homologue
    • 23 June
    • Akyuz, N. et al. Transport dynamics in a glutamate transporter homologue. Nature http://dx.doi.org/10.1038/nature12265 (23 June 2013).
    • (2013) Nature
    • Akyuz, N.1
  • 16
    • 78650476908 scopus 로고    scopus 로고
    • Aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: Implications for detergent-solubilized membrane proteins
    • Dorwart, M. R. et al. S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: implications for detergent-solubilized membrane proteins. PLoS Biol. 8, e1000555 (2010).
    • (2010) PLoS Biol. , vol.8
    • Dorwart, M.R.1    Et Al., S.2
  • 17
    • 77955133265 scopus 로고    scopus 로고
    • Analysis of kinetic intermediates in single-particle dwell-time distributions
    • Floyd, D. L., Harrison, S. C. & van Oijen, A. M. Analysis of kinetic intermediates in single-particle dwell-time distributions. Biophys. J. 99, 360-366 (2010).
    • (2010) Biophys. J. , vol.99 , pp. 360-366
    • Floyd, D.L.1    Harrison, S.C.2    Van Oijen, A.M.3
  • 18
    • 14044263640 scopus 로고    scopus 로고
    • Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters
    • Koch, H. P. & Larsson, H. P. Small-scale molecular motions accomplish glutamate uptake in human glutamate transporters. J. Neurosci. 25, 1730-1736 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 1730-1736
    • Koch, H.P.1    Larsson, H.P.2
  • 19
    • 24344507684 scopus 로고    scopus 로고
    • Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other
    • Grewer, C. et al. Individual subunits of the glutamate transporter EAAC1 homotrimer function independently of each other. Biochemistry 44, 11913-11923 (2005).
    • (2005) Biochemistry , vol.44 , pp. 11913-11923
    • Grewer, C.1
  • 20
    • 33947318986 scopus 로고    scopus 로고
    • The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits
    • Koch, H. P., Brown, R. L. & Larsson, H. P. The glutamate-activated anion conductance in excitatory amino acid transporters is gated independently by the individual subunits. J. Neurosci. 27, 2943-2947 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 2943-2947
    • Koch, H.P.1    Brown, R.L.2    Larsson, H.P.3
  • 21
    • 4444313551 scopus 로고    scopus 로고
    • TRNAdynamics on the ribosome during translation
    • USA
    • Blanchard, S. C. et al. tRNAdynamics on the ribosome during translation. Proc.Natl Acad. Sci. USA 101, 12893-12898 (2004).
    • (2004) Proc.Natl Acad. Sci. , vol.101 , pp. 12893-12898
    • Blanchard, S.C.1
  • 22
    • 0034691129 scopus 로고    scopus 로고
    • Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane
    • USA
    • van der Heide, T. & Poolman, B. Osmoregulated ABC-transport system of Lactococcus lactis senses water stress via changes in the physical state of the membrane. Proc. Natl Acad. Sci. USA 97, 7102-7106 (2000).
    • (2000) Proc. Natl Acad. Sci. , vol.97 , pp. 7102-7106
    • Van Der Heide, T.1    Poolman, B.2
  • 23
    • 77954575187 scopus 로고    scopus 로고
    • VisualizingDNA replication at the single-molecule level
    • Tanner, N. A.&van Oijen, A. M. VisualizingDNA replication at the single-molecule level. Methods Enzymol. 475, 259-278 (2010).
    • (2010) Methods Enzymol. , vol.475 , pp. 259-278
    • Tanner, N.A.1    Van Oijen, A.M.2
  • 24
    • 67749103813 scopus 로고    scopus 로고
    • On the mechanism of Trolox as antiblinking and antibleaching reagent
    • Cordes, T., Vogelsang, J. & Tinnefeld, P. On the mechanism of Trolox as antiblinking and antibleaching reagent. J. Am. Chem. Soc. 131, 5018-5019 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5018-5019
    • Cordes, T.1    Vogelsang, J.2    Tinnefeld, P.3
  • 25
    • 23744455796 scopus 로고    scopus 로고
    • Alternating-laser excitation of single molecules
    • Kapanidis, A. N. et al. Alternating-laser excitation of single molecules. Acc. Chem. Res. 38, 523-533 (2005).
    • (2005) Acc. Chem. Res. , vol.38 , pp. 523-533
    • Kapanidis, A.N.1
  • 26
    • 40149088424 scopus 로고    scopus 로고
    • Efficient subpixel image registration algorithms
    • Guizar-Sicairos, M., Thurman, S. T. & Fienup, J. R. Efficient subpixel image registration algorithms. Opt. Lett. 33, 156-158 (2008).
    • (2008) Opt. Lett. , vol.33 , pp. 156-158
    • Guizar-Sicairos, M.1    Thurman, S.T.2    Fienup, J.R.3
  • 27
    • 0030212172 scopus 로고    scopus 로고
    • An FFT-based technique for translation, rotation, and scale-invariant imageregistration
    • Reddy, B. S. & Chatterji, B. N. An FFT-based technique for translation, rotation, and scale-invariant imageregistration. IEEE Trans. ImageProcess. 5,1266-1271(1996).
    • (1996) IEEE Trans. ImageProcess. , vol.5 , pp. 1266-1271
    • Reddy, B.S.1    Chatterji, B.N.2
  • 28
    • 70349629402 scopus 로고    scopus 로고
    • Online image analysis software for photoactivation localization microscopy
    • Hedde, P. N. et al. Online image analysis software for photoactivation localization microscopy. Nature Methods 6, 689-690 (2009).
    • (2009) Nature Methods , vol.6 , pp. 689-690
    • Hedde, P.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.