Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters

Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Mary Hongying Cheng [verfasserIn] Delany Torres-Salazar [verfasserIn] Aneysis D Gonzalez-Suarez [verfasserIn] Susan G Amara [verfasserIn] Ivet Bahar [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii

Übergeordnetes Werk:	In: eLife - eLife Sciences Publications Ltd, 2013, 6(2017)
Übergeordnetes Werk:	volume:6 ; year:2017

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.7554/eLife.25850

Katalog-ID:	DOAJ00445538X

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allfields	10.7554/eLife.25850 doi (DE-627)DOAJ00445538X (DE-599)DOAJ84267c63cddb4bf2905edf38e175038c DE-627 ger DE-627 rakwb eng QH301-705.5 Mary Hongying Cheng verfasserin aut Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions. human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii Medicine R Science Q Biology (General) Delany Torres-Salazar verfasserin aut Aneysis D Gonzalez-Suarez verfasserin aut Susan G Amara verfasserin aut Ivet Bahar verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.25850 kostenfrei https://doaj.org/article/84267c63cddb4bf2905edf38e175038c kostenfrei https://elifesciences.org/articles/25850 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
spelling	10.7554/eLife.25850 doi (DE-627)DOAJ00445538X (DE-599)DOAJ84267c63cddb4bf2905edf38e175038c DE-627 ger DE-627 rakwb eng QH301-705.5 Mary Hongying Cheng verfasserin aut Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions. human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii Medicine R Science Q Biology (General) Delany Torres-Salazar verfasserin aut Aneysis D Gonzalez-Suarez verfasserin aut Susan G Amara verfasserin aut Ivet Bahar verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.25850 kostenfrei https://doaj.org/article/84267c63cddb4bf2905edf38e175038c kostenfrei https://elifesciences.org/articles/25850 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
allfields_unstemmed	10.7554/eLife.25850 doi (DE-627)DOAJ00445538X (DE-599)DOAJ84267c63cddb4bf2905edf38e175038c DE-627 ger DE-627 rakwb eng QH301-705.5 Mary Hongying Cheng verfasserin aut Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions. human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii Medicine R Science Q Biology (General) Delany Torres-Salazar verfasserin aut Aneysis D Gonzalez-Suarez verfasserin aut Susan G Amara verfasserin aut Ivet Bahar verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.25850 kostenfrei https://doaj.org/article/84267c63cddb4bf2905edf38e175038c kostenfrei https://elifesciences.org/articles/25850 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
allfieldsGer	10.7554/eLife.25850 doi (DE-627)DOAJ00445538X (DE-599)DOAJ84267c63cddb4bf2905edf38e175038c DE-627 ger DE-627 rakwb eng QH301-705.5 Mary Hongying Cheng verfasserin aut Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions. human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii Medicine R Science Q Biology (General) Delany Torres-Salazar verfasserin aut Aneysis D Gonzalez-Suarez verfasserin aut Susan G Amara verfasserin aut Ivet Bahar verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.25850 kostenfrei https://doaj.org/article/84267c63cddb4bf2905edf38e175038c kostenfrei https://elifesciences.org/articles/25850 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
allfieldsSound	10.7554/eLife.25850 doi (DE-627)DOAJ00445538X (DE-599)DOAJ84267c63cddb4bf2905edf38e175038c DE-627 ger DE-627 rakwb eng QH301-705.5 Mary Hongying Cheng verfasserin aut Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions. human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii Medicine R Science Q Biology (General) Delany Torres-Salazar verfasserin aut Aneysis D Gonzalez-Suarez verfasserin aut Susan G Amara verfasserin aut Ivet Bahar verfasserin aut In eLife eLife Sciences Publications Ltd, 2013 6(2017) (DE-627)728518384 (DE-600)2687154-3 2050084X nnns volume:6 year:2017 https://doi.org/10.7554/eLife.25850 kostenfrei https://doaj.org/article/84267c63cddb4bf2905edf38e175038c kostenfrei https://elifesciences.org/articles/25850 kostenfrei https://doaj.org/toc/2050-084X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 2017
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authorswithroles_txt_mv	Mary Hongying Cheng @@aut@@ Delany Torres-Salazar @@aut@@ Aneysis D Gonzalez-Suarez @@aut@@ Susan G Amara @@aut@@ Ivet Bahar @@aut@@
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callnumber-first	Q - Science
author	Mary Hongying Cheng
spellingShingle	Mary Hongying Cheng misc QH301-705.5 misc human excitatory amino acid transporter 1 misc anion channeling misc Aspartate transporter from Pyrococcus horikoshii misc Medicine misc R misc Science misc Q misc Biology (General) Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
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topic_title	QH301-705.5 Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters human excitatory amino acid transporter 1 anion channeling Aspartate transporter from Pyrococcus horikoshii
topic	misc QH301-705.5 misc human excitatory amino acid transporter 1 misc anion channeling misc Aspartate transporter from Pyrococcus horikoshii misc Medicine misc R misc Science misc Q misc Biology (General)
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title	Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
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title_full	Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
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title_sort	substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
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title_auth	Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
abstract	Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions.
abstractGer	Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions.
abstract_unstemmed	Advances in structure-function analyses and computational biology have enabled a deeper understanding of how excitatory amino acid transporters (EAATs) mediate chloride permeation and substrate transport. However, the mechanism of structural coupling between these functions remains to be established. Using a combination of molecular modeling, substituted cysteine accessibility, electrophysiology and glutamate uptake assays, we identified a chloride-channeling conformer, iChS, transiently accessible as EAAT1 reconfigures from substrate/ion-loaded into a substrate-releasing conformer. Opening of the anion permeation path in this iChS is controlled by the elevator-like movement of the substrate-binding core, along with its wall that simultaneously lines the anion permeation path (global); and repacking of a cluster of hydrophobic residues near the extracellular vestibule (local). Moreover, our results demonstrate that stabilization of iChS by chemical modifications favors anion channeling at the expense of substrate transport, suggesting a mutually exclusive regulation mediated by the movement of the flexible wall lining the two regions.
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title_short	Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters
url	https://doi.org/10.7554/eLife.25850 https://doaj.org/article/84267c63cddb4bf2905edf38e175038c https://elifesciences.org/articles/25850 https://doaj.org/toc/2050-084X
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author2	Delany Torres-Salazar Aneysis D Gonzalez-Suarez Susan G Amara Ivet Bahar
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up_date	2024-07-03T23:48:05.003Z
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Substrate transport and anion permeation proceed through distinct pathways in glutamate transporters

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