In:
eLife, eLife Sciences Publications, Ltd, Vol. 6 ( 2017-01-24)
Abstract:
All living cells need amino acids – the building blocks of proteins – in order to survive, yet few cells can make all the amino acids that they need. Instead, transporter proteins in cell membranes must take these molecules from the outside of the cell and release them to the inside. Some cells, including those in the brain, also release amino acids and molecules derived from them into the spaces outside of the cell to send signals to other nearby cells. Again, transporter proteins must move these signaling molecules back inside cells, to stop the signaling and to allow the molecules to be recycled. Importantly, problems with these uptake mechanisms have been linked to disorders such as depression, epilepsy and Parkinson’s disease. One family of transporters involved in the uptake of amino acids are the “Neurotransmitter:Sodium Symporters”. Though these proteins are involved in processes that are fundamental to life, it remains unclear exactly how they work. Specifically, it has been heavily debated whether this family of transporters require one or two amino acid molecules to bind at the same time in order to help transport them across the membrane. Now Erlendsson, Gotfryd et al. have analyzed a bacterial protein in the Neurotransmitter:Sodium Symporter family. This transporter takes up an amino acid called leucine into cells, and is commonly used as a model to understand this family of transporter proteins more generally. Using a technique called solid state nuclear magnetic resonance, Erlendsson, Gotfryd et al. could detect a single molecule of leucine bound to each transporter, but not a second one. This technique could also pinpoint that the leucine was located at the transporter’s central binding site. Leucine was never found at the proposed secondary binding site. Together these findings suggest that only one molecule of leucine binds to the transporter at any one time, and that it binds to the transporter’s central binding site. Erlendsson, Gotfryd et al. have shown now how solid state nuclear magnetic resonance can be used to explore in detail how Neurotransmitter:Sodium Symporters move molecules across cell membranes. The next challenge is to use the same experimental setup to characterize other Neurotransmitter:Sodium Symporters. Doing so could potentially lay the groundwork for designing more specific and improved drugs to treat disorders like depression and Parkinson’s disease.
Type of Medium:
Online Resource
ISSN:
2050-084X
DOI:
10.7554/eLife.19314.001
DOI:
10.7554/eLife.19314.002
DOI:
10.7554/eLife.19314.003
DOI:
10.7554/eLife.19314.004
DOI:
10.7554/eLife.19314.005
DOI:
10.7554/eLife.19314.006
DOI:
10.7554/eLife.19314.007
DOI:
10.7554/eLife.19314.008
DOI:
10.7554/eLife.19314.009
DOI:
10.7554/eLife.19314.010
DOI:
10.7554/eLife.19314.011
DOI:
10.7554/eLife.19314.012
DOI:
10.7554/eLife.19314.013
DOI:
10.7554/eLife.19314.014
DOI:
10.7554/eLife.19314.015
DOI:
10.7554/eLife.19314.016
Language:
English
Publisher:
eLife Sciences Publications, Ltd
Publication Date:
2017
detail.hit.zdb_id:
2687154-3
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