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. 2020 Feb 28;10:3731. doi: 10.1038/s41598-020-60617-y

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Central role of Asc-1 at the tripartite glutamatergic synapse. (a) It has been reported that the Asc-1 transporter (blue) plays an important role in regulating NMDAR-dependent synaptic activity by mediating release of d-serine (red) in exchange to other neutral amino acids (violet) including glycine (yellow). Activation of the GluN1-GluN2 containing NMDA receptors (NMDAR, grey) in addition to glutamate requires the binding of a co-agonist d-serine and/or glycine. Interestingly, the binding of glycine overlaps with the d-serine binding at synaptic NMDARs. Also, d-serine is formed from l-serine by Serine Racemase (SR, green). Transport of d-serine including the efflux of the substrate (indicated by M1 mechanism) along with the uptake of the substrate (indicated by M2 mechanism) across the membrane involves roughly three states: outward-open (OO), occluded (O) and inward-open (IO) (Fig. 1b) with additional intermediate states such as outward-open occluded (OOO) and inward-open occluded (IOO) (not shown).