Structural characterisation reveals insights into substrate recognition by the glutamine transporter ASCT2/SLC1A5
Cancer cells are reliant on nutrients such as glutamine, which enter the cell via the alanine/serine/cysteine transporter 2 (ASCT2). Here, authors use crystallography to show which amino-acid residues in the substrate-binding site are responsible for conferring glutamine selectivity to ASCT2.
Main Authors: | Amanda J Scopelliti, Josep Font, Robert J Vandenberg, Olga Boudker, Renae M Ryan |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2018-01-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-017-02444-w |
Similar Items
-
Cryo-EM structures of the human glutamine transporter SLC1A5 (ASCT2) in the outward-facing conformation
by: Xiaodi Yu, et al.
Published: (2019-10-01) -
Cryo-EM structures of the human glutamine transporter SLC1A5 (ASCT2) in the outward-facing conformation
by: Yu, X, et al.
Published: (2019) -
Research Progress of Glutamine Transporter ASCT2 in Cancer
by: WANG Yale, et al.
Published: (2019-03-01) -
Homology Modeling Informs Ligand Discovery for the Glutamine Transporter ASCT2
by: Rachel-Ann A. Garibsingh, et al.
Published: (2018-07-01) -
D-Serine Is a Substrate for Neutral Amino Acid Transporters ASCT1/SLC1A4 and ASCT2/SLC1A5, and Is Transported by Both Subtypes in Rat Hippocampal Astrocyte Cultures.
by: Alan C Foster, et al.
Published: (2016-01-01)