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  Vesicular glutamate transporters use flexible anion and cation binding sites for efficient accumulation of neurotransmitter.

Preobraschenski, J., Zander, J. F., Suzuki, T., Ahnert-Hilger, G., & Jahn, R. (2014). Vesicular glutamate transporters use flexible anion and cation binding sites for efficient accumulation of neurotransmitter. Neuron, 84(6), 1287-1301. doi:10.1016/j.neuron.2014.11.008.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-B9AF-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-0B2E-3
Genre: Journal Article

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Preobraschenski, J.1, Author              
Zander, J. F., Author
Suzuki, T., Author
Ahnert-Hilger, G., Author
Jahn, R.1, Author              
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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 Abstract: Vesicular glutamate transporters (VGLUTs) accumulate the neurotransmitter glutamate in synaptic vesicles. Transport depends on a V-ATPase-dependent electrochemical proton gradient (Delta mu H+) and requires chloride ions, but how chloride acts and how ionic and charge balance is maintained during transport is controversial. Using a reconstitution approach, we used an exogenous proton pump to drive VGLUT-mediated transport either in liposomes containing purified VGLUT1 or in synaptic vesicles fused with proton-pump-containing liposomes. Our data show that chloride stimulation can be induced at both sides of the membrane. Moreover, chloride competes with glutamate at high concentrations. In addition, VGLUT1 possesses a cation binding site capable of binding H+ or K+ ions, allowing for proton antiport or K+/H+ exchange. We conclude that VGLUTs contain two anion binding sites and one cation binding site, allowing the transporter to adjust to the changing ionic conditions during vesicle filling without being dependent on other transporters or channels.

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Language(s): eng - English
 Dates: 2014-11-262014-12-14
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.neuron.2014.11.008
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Title: Neuron
Source Genre: Journal
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Pages: - Volume / Issue: 84 (6) Sequence Number: - Start / End Page: 1287 - 1301 Identifier: -