Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/165343
Title: Functional characterization of the alanine-serine-cysteine exchanger of Carnobacterium sp AT7
Author: Bartoccioni, Paola
Fort Joana
Zorzano Olarte, Antonio
Errasti-Murugarren, Ekaitz
Palacín Prieto, Manuel
Keywords: Cèl·lules
Aminoàcids
Proteïnes
Cells
Amino acids
Proteins
Issue Date: 1-Apr-2019
Publisher: Rockefeller University Press
Abstract: Many key cell processes require prior cell uptake of amino acids from the environment, which is facilitated by cell membrane amino acid transporters such as those of the L-type amino acid transporter (LAT) subfamily. Alterations in LAT subfamily amino acid transport are associated with several human diseases, including cancer, aminoacidurias, and neurodegenerative conditions. Therefore, from the perspective of human health, there is considerable interest in obtaining structural information about these transporter proteins. We recently solved the crystal structure of the first LAT transporter, the bacterial alanine-serine-cysteine exchanger of Carnobacterium sp AT7 (BasC). Here, we provide a complete functional characterization of detergent-purified, liposome-reconstituted BasC transporter to allow the extension of the structural insights into mechanistic understanding. BasC is a sodium- and proton-independent small neutral amino acid exchanger whose substrate and inhibitor selectivity are almost identical to those previously described for the human LAT subfamily member Asc-1. Additionally, we show that, like its human counterparts, this transporter has apparent affinity asymmetry for the intra- and extracellular substrate binding sites a key feature in the physiological role played by these proteins. BasC is an excellent paradigm of human LAT transporters and will contribute to our understanding of the molecular mechanisms underlying substrate recognition and translocation at both sides of the plasma membrane.
Note: Reproducció del document publicat a: https://doi.org/10.1085/jgp.201812195
It is part of: Journal of General Physiology, 2019, vol. 151, num. 4, p. 505-517
URI: http://hdl.handle.net/2445/165343
Related resource: https://doi.org/10.1085/jgp.201812195
ISSN: 0022-1295
Appears in Collections:Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

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