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Title: Cryo-EM structure of the human neutral amino acid transporter ASCT2

Abstract

Human ASCT2 belongs to the SLC1 family of secondary transporters and is specific for the transport of small neutral amino acids. ASCT2 is upregulated in cancer cells and serves as the receptor for many retroviruses; hence, it has importance as a potential drug target. Here we used single-particle cryo-EM to determine a structure of the functional and unmodified human ASCT2 at 3.85-Å resolution. ASCT2 forms a homotrimeric complex in which each subunit contains a transport and a scaffold domain. Prominent extracellular extensions on the scaffold domain form the predicted docking site for retroviruses. Relative to structures of other SLC1 members, ASCT2 is in the most extreme inward-oriented state, with the transport domain largely detached from the central scaffold domain on the cytoplasmic side. In conclusion, this domain detachment may be required for substrate binding and release on the intracellular side of the membrane.

Authors:
 [1]; ORCiD logo [1];  [2]; ORCiD logo [1];  [1]; ORCiD logo [1]
+ Show Author Affiliations
  1. Univ. of Groningen, Groningen (The Netherlands)
  2. SLAC National Accelerator Lab., Menlo Park, CA (United States); Stanford Univ., Stanford, CA (United States)
Publication Date:
Research Org.:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1475494
Grant/Contract Number:  
AC02-76SF00515
Resource Type:
Accepted Manuscript
Journal Name:
Nature Structural & Molecular Biology
Additional Journal Information:
Journal Volume: 25; Journal Issue: 6; Journal ID: ISSN 1545-9993
Publisher:
Nature Publishing Group
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Garaeva, Alisa A., Oostergetel, Gert T., Gati, Cornelius, Guskov, Albert, Paulino, Cristina, and Slotboom, Dirk J. Cryo-EM structure of the human neutral amino acid transporter ASCT2. United States: N. p., 2018. Web. doi:10.1038/s41594-018-0076-y.
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Garaeva, Alisa A., Oostergetel, Gert T., Gati, Cornelius, Guskov, Albert, Paulino, Cristina, & Slotboom, Dirk J. Cryo-EM structure of the human neutral amino acid transporter ASCT2. United States. https://doi.org/10.1038/s41594-018-0076-y
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Garaeva, Alisa A., Oostergetel, Gert T., Gati, Cornelius, Guskov, Albert, Paulino, Cristina, and Slotboom, Dirk J. Tue . "Cryo-EM structure of the human neutral amino acid transporter ASCT2". United States. https://doi.org/10.1038/s41594-018-0076-y. https://www.osti.gov/servlets/purl/1475494.
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@article{osti_1475494,
title = {Cryo-EM structure of the human neutral amino acid transporter ASCT2},
author = {Garaeva, Alisa A. and Oostergetel, Gert T. and Gati, Cornelius and Guskov, Albert and Paulino, Cristina and Slotboom, Dirk J.},
abstractNote = {Human ASCT2 belongs to the SLC1 family of secondary transporters and is specific for the transport of small neutral amino acids. ASCT2 is upregulated in cancer cells and serves as the receptor for many retroviruses; hence, it has importance as a potential drug target. Here we used single-particle cryo-EM to determine a structure of the functional and unmodified human ASCT2 at 3.85-Å resolution. ASCT2 forms a homotrimeric complex in which each subunit contains a transport and a scaffold domain. Prominent extracellular extensions on the scaffold domain form the predicted docking site for retroviruses. Relative to structures of other SLC1 members, ASCT2 is in the most extreme inward-oriented state, with the transport domain largely detached from the central scaffold domain on the cytoplasmic side. In conclusion, this domain detachment may be required for substrate binding and release on the intracellular side of the membrane.},
doi = {10.1038/s41594-018-0076-y},
journal = {Nature Structural & Molecular Biology},
number = 6,
volume = 25,
place = {United States},
year = {Tue Jun 05 00:00:00 EDT 2018},
month = {Tue Jun 05 00:00:00 EDT 2018}
}
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Journal Article:
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Publisher's Version of Record
https://doi.org/10.1038/s41594-018-0076-y
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Cited by: 85 works
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Figures / Tables:

Fig. 1 Fig. 1: Functional characterization of ASCT2. a, Exchange of internal unlabeled glutamine with external [ 3H]glutamine, and inhibition of transport by addition of an excess of unlabeled amino acids (circle, glutamine; diamond, tryptophan; X, no externally added amino acid (No)). b, Inhibitory effect of externally added amino acids. c, Exchangemore » of internal amino acid substrate. d, Ability of alternative internal amino acids to drive uptake of glutamine. e, Electroneutral nature of exchange and sodium dependency. Circle, 3 $μ$M valinomycin was added at 23 min to proteoliposomes with a 100-fold K+ gradient; downward triangle, ethanol was added at 23 min to proteoliposomes with a 100-fold K+ gradient; square, 3 $μ$M valinomycin was added at the start to proteoliposomes with a 100-fold K+ gradient; upward triangle, proteoliposomes in the absence of Na+. Arrow indicates time of addition of valinomycin or ethanol (23 min). f, Exchange of internal unlabeled glutamine with external [ 3H]glutamine in proteoliposomes containing different amounts of cholesterol. Circle, proteoliposomes without cholesterol; downward triangle, with 5% (wt/wt) cholesterol; square, with 10% (wt/wt) cholesterol. Data points and error bars represent means± s.e.m. from 3 biologically independent experiments, each done in one technical replicate. Small schemes in the top left corners of a, c, e and f schematically represent proteoliposomes with internal and external compound compositions used in corresponding experiments.« less
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