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Rush Hour of LATs towards Their Transport Cycle

The mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In...

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Autores principales: Nicolàs-Aragó, Adrià, Fort, Joana, Palacín, Manuel, Errasti-Murugarren, Ekaitz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8399266/
https://www.ncbi.nlm.nih.gov/pubmed/34436365
http://dx.doi.org/10.3390/membranes11080602
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author Nicolàs-Aragó, Adrià
Fort, Joana
Palacín, Manuel
Errasti-Murugarren, Ekaitz
author_facet Nicolàs-Aragó, Adrià
Fort, Joana
Palacín, Manuel
Errasti-Murugarren, Ekaitz
author_sort Nicolàs-Aragó, Adrià
collection PubMed
description The mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In the last four years, several crystal or cryo-EM structures of LATs and CATs have been solved. These structures have started to fill our knowledge gap that previously was based on the structural biology of remote homologs of the amino acid–polyamine–organocation (APC) transporters. This review recovers this structural and functional information to start generating the molecular bases of the transport cycle of LATs. Special attention is given to the known transporter conformations within the transport cycle and the molecular bases for substrate interaction and translocation, including the asymmetric interaction of substrates at both sides of the plasma membrane.
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spelling pubmed-83992662021-08-29 Rush Hour of LATs towards Their Transport Cycle Nicolàs-Aragó, Adrià Fort, Joana Palacín, Manuel Errasti-Murugarren, Ekaitz Membranes (Basel) Review The mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In the last four years, several crystal or cryo-EM structures of LATs and CATs have been solved. These structures have started to fill our knowledge gap that previously was based on the structural biology of remote homologs of the amino acid–polyamine–organocation (APC) transporters. This review recovers this structural and functional information to start generating the molecular bases of the transport cycle of LATs. Special attention is given to the known transporter conformations within the transport cycle and the molecular bases for substrate interaction and translocation, including the asymmetric interaction of substrates at both sides of the plasma membrane. MDPI 2021-08-08 /pmc/articles/PMC8399266/ /pubmed/34436365 http://dx.doi.org/10.3390/membranes11080602 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Nicolàs-Aragó, Adrià
Fort, Joana
Palacín, Manuel
Errasti-Murugarren, Ekaitz
Rush Hour of LATs towards Their Transport Cycle
title Rush Hour of LATs towards Their Transport Cycle
title_full Rush Hour of LATs towards Their Transport Cycle
title_fullStr Rush Hour of LATs towards Their Transport Cycle
title_full_unstemmed Rush Hour of LATs towards Their Transport Cycle
title_short Rush Hour of LATs towards Their Transport Cycle
title_sort rush hour of lats towards their transport cycle
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8399266/
https://www.ncbi.nlm.nih.gov/pubmed/34436365
http://dx.doi.org/10.3390/membranes11080602
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