Tryptophan-Starved Human Cells Overexpressing Tryptophanyl-tRNA Synthetase Enhance High-Affinity Tryptophan Uptake via Enzymatic Production of Tryptophanyl-AMP.
amino acid transport
aminoacyl-tRNA synthetase
mutagenesis
tryptophan
tryptophan depletion
tryptophanyl-tRNA synthetase
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
22 Oct 2023
22 Oct 2023
Historique:
received:
13
09
2023
revised:
18
10
2023
accepted:
21
10
2023
medline:
30
10
2023
pubmed:
28
10
2023
entrez:
28
10
2023
Statut:
epublish
Résumé
Our previous study demonstrated that L-tryptophan (Trp)-depleted cells display a marked enhancement in Trp uptake facilitated by extracellular tryptophanyl-tRNA synthetase (TrpRS). Here, we show that Trp uptake into TrpRS-overexpressing cells is also markedly elevated upon Trp starvation. These findings indicate that a Trp-deficient condition is critical for Trp uptake, not only into cells to which TrpRS protein has been added but also into TrpRS-overexpressing cells. We also show that overexpression of TrpRS mutants, which cannot synthesize tryptophanyl-AMP, does not promote Trp uptake, and that inhibition of tryptophanyl-AMP synthesis suppresses this uptake. Overall, these data suggest that tryptophanyl-AMP production by TrpRS is critical for high-affinity Trp uptake.
Identifiants
pubmed: 37895133
pii: ijms242015453
doi: 10.3390/ijms242015453
pmc: PMC10607379
pii:
doi:
Substances chimiques
Tryptophan
8DUH1N11BX
Tryptophan-tRNA Ligase
EC 6.1.1.2
WARS1 protein, human
EC 6.1.1.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Japan Society for the Promotion of Science
ID : 20K06537
Organisme : Japan Society for the Promotion of Science
ID : 22H05559
Organisme : Smoking Research Foundation
ID : 2022G002
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