Lysine 204 is crucial for the antiport function of the human LAT1 transporter.
Amino acids
Antiport
Liposomes
Molecular dynamics
SLC
Uniport
Journal
Biochimica et biophysica acta. Bioenergetics
ISSN: 1879-2650
Titre abrégé: Biochim Biophys Acta Bioenerg
Pays: Netherlands
ID NLM: 101731706
Informations de publication
Date de publication:
18 Oct 2024
18 Oct 2024
Historique:
received:
15
05
2024
revised:
11
07
2024
accepted:
15
10
2024
medline:
21
10
2024
pubmed:
21
10
2024
entrez:
20
10
2024
Statut:
aheadofprint
Résumé
LAT1 (SLC7A5) catalyzes an antiport reaction of amino acids with specificity towards the essential ones. It is mainly expressed at the Blood Brain Barrier and placenta barriers, but it becomes over-expressed in virtually all human cancers even if originating from tissues with lower expression levels. The antiport reaction of LAT1 is crucial at the BBB since its inherited loss causes Autism Spectrum Disorder. We have investigated the possible molecular determinant of the antiport by site-directed mutagenesis, in vitro transport assay and computational analysis. Previous data indicated that mutation of K204 impairs, but does not knock out LAT1 functionality. We have investigated the activity changes in the K204Q mutant by following the transport of [
Identifiants
pubmed: 39428051
pii: S0005-2728(24)00490-0
doi: 10.1016/j.bbabio.2024.149520
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
149520Informations de copyright
Copyright © 2024. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.