Amb motiu del tancament d'estiu, la validació de documents es reprendrà a partir del 28 d'agost de 2026. Disculpeu les molèsties.
Con motivo del cierre de verano, la validación de documentos se reanudará a partir del 28 de agosto de 2026. Disculpad las molestias
Due to the summer closure, document validation will resume starting August 28, 2026. We apologize for any inconvenience.

Files

687055.pdf (2.1 MB)

Document type

Article

Version

Published version

Publication date

2019-04-01

Publication license

cc-by-nc-sa (c) Bartoccioni, Paola et al., 2019
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/165343

Functional characterization of the alanine-serine-cysteine exchanger of Carnobacterium sp AT7

Journal Title

Authors

Director/Tutor

Journal ISSN

Volume Title

Related resource

https://doi.org/10.1085/jgp.201812195

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.

Subject

Cèl·lules, Aminoàcids, Proteïnes

Subject (English)

Cells, Amino acids, Proteins

Citation

Collections

Articles publicats en revistes (Bioquímica i Biomedicina Molecular)

Citation

BARTOCCIONI, Paola, et al. Functional characterization of the alanine-serine-cysteine exchanger of Carnobacterium sp AT7. Journal of General Physiology. 2019. Vol. 151, num. 4, pags. 505-517. ISSN 0022-1295. [consulted: 10 of August of 2026]. Available at: https://hdl.handle.net/2445/165343

Export metadata

JSON - METS

Share record