Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter

Christian B. Billesbølle; Mie B. Krüger; Lei Shi; Matthias Quick; Zheng Li; Sebastian Stolzenberg; Julie Kniazeff; Kamil Gotfryd; Jonas S. Mortensen; Jonathan A. Javitch; Harel Weinstein; Claus J. Loland; Ulrik Gether

doi:10.1074/jbc.M115.677658

Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter

Christian B. Billesbølle, Mie B. Krüger, Lei Shi, Matthias Quick, Zheng Li, Sebastian Stolzenberg, Julie Kniazeff, Kamil Gotfryd, Jonas S. Mortensen, Jonathan A. Javitch, Harel Weinstein, Claus J. Loland, Ulrik Gether

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

Background: The mechanism coupling substrate binding to transport in neurotransmitter: sodium symporters (NSSs) is poorly understood. Results: Site-directed fluorescence quenching spectroscopy experiments on the NSS homologue LeuT reveal a structural intermediate preceding transition to the inward-open conformation. Conclusion: Stability of the intermediate might represent a rate-limiting barrier in the transport mechanism. Significance: The data add to our mechanistic understanding of Na+-coupled transport across lipid bilayers.

Original language	English (US)
Pages (from-to)	26725-26738
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	290
Issue number	44
DOIs	https://doi.org/10.1074/jbc.M115.677658
State	Published - Oct 30 2015

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Billesbølle, C. B., Krüger, M. B., Shi, L., Quick, M., Li, Z., Stolzenberg, S., Kniazeff, J., Gotfryd, K., Mortensen, J. S., Javitch, J. A., Weinstein, H., Loland, C. J., & Gether, U. (2015). Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter. Journal of Biological Chemistry, 290(44), 26725-26738. https://doi.org/10.1074/jbc.M115.677658

Billesbølle, CB, Krüger, MB, Shi, L, Quick, M, Li, Z, Stolzenberg, S, Kniazeff, J, Gotfryd, K, Mortensen, JS, Javitch, JA, Weinstein, H, Loland, CJ & Gether, U 2015, 'Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter', Journal of Biological Chemistry, vol. 290, no. 44, pp. 26725-26738. https://doi.org/10.1074/jbc.M115.677658

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title = "Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter",

abstract = "Background: The mechanism coupling substrate binding to transport in neurotransmitter: sodium symporters (NSSs) is poorly understood. Results: Site-directed fluorescence quenching spectroscopy experiments on the NSS homologue LeuT reveal a structural intermediate preceding transition to the inward-open conformation. Conclusion: Stability of the intermediate might represent a rate-limiting barrier in the transport mechanism. Significance: The data add to our mechanistic understanding of Na+-coupled transport across lipid bilayers.",

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doi = "10.1074/jbc.M115.677658",

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AU - Quick, Matthias

AU - Li, Zheng

AU - Stolzenberg, Sebastian

AU - Kniazeff, Julie

AU - Gotfryd, Kamil

AU - Mortensen, Jonas S.

AU - Javitch, Jonathan A.

AU - Weinstein, Harel

AU - Loland, Claus J.

AU - Gether, Ulrik

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AB - Background: The mechanism coupling substrate binding to transport in neurotransmitter: sodium symporters (NSSs) is poorly understood. Results: Site-directed fluorescence quenching spectroscopy experiments on the NSS homologue LeuT reveal a structural intermediate preceding transition to the inward-open conformation. Conclusion: Stability of the intermediate might represent a rate-limiting barrier in the transport mechanism. Significance: The data add to our mechanistic understanding of Na+-coupled transport across lipid bilayers.

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Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter: Sodium symporter

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