Substrate-induced differential degradation and partitioning of the two tryptophan permeases Tat1 and Tat2 into eisosomes in Saccharomyces cerevisiae.
Amino Acid Transport Systems
/ genetics
Endosomal Sorting Complexes Required for Transport
/ metabolism
Kinetics
Mutagenesis, Site-Directed
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ genetics
Substrate Specificity
Tryptophan
/ chemistry
Tyrosine
/ chemistry
Ubiquitin-Protein Ligase Complexes
/ metabolism
Ubiquitination
Degradation
Eisosomes
Pil1
Rsp5-Bul1 complex
Saccharomyces cerevisiae
Tat1
Tat2
Tryptophan permease
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 04 2022
01 04 2022
Historique:
received:
08
09
2021
revised:
22
12
2021
accepted:
27
12
2021
pubmed:
16
1
2022
medline:
11
3
2022
entrez:
15
1
2022
Statut:
ppublish
Résumé
Tryptophan is a relatively rare amino acid whose influx is strictly controlled to meet cellular demands. The yeast Saccharomyces cerevisiae has two tryptophan permeases, namely Tat1 (low-affinity type) and Tat2 (high-affinity type). These permeases are differentially regulated through ubiquitination based on inducible conditions and dependence on arrestin-related trafficking adaptors, although the physiological significance of their degradation remain unclear. Here, we demonstrated that Tat2 was rapidly degraded in an Rsp5-Bul1-dependent manner upon the addition of tryptophan, phenylalanine, or tyrosine, whereas Tat1 was unaffected. The expression of the ubiquitination-deficient variant Tat2
Identifiants
pubmed: 35031272
pii: S0005-2736(21)00307-2
doi: 10.1016/j.bbamem.2021.183858
pii:
doi:
Substances chimiques
Amino Acid Transport Systems
0
Endosomal Sorting Complexes Required for Transport
0
Saccharomyces cerevisiae Proteins
0
TAT1 protein, S cerevisiae
0
TAT2 protein, S cerevisiae
0
Tyrosine
42HK56048U
Tryptophan
8DUH1N11BX
Ubiquitin-Protein Ligase Complexes
EC 2.3.2.23
RSP5 protein, S cerevisiae
EC 6.3.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
183858Informations de copyright
Copyright © 2022 Elsevier B.V. All rights reserved.