Substrate-induced differential degradation and partitioning of the two tryptophan permeases Tat1 and Tat2 into eisosomes in Saccharomyces cerevisiae.


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
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

183858

Informations de copyright

Copyright © 2022 Elsevier B.V. All rights reserved.

Auteurs

Ryoga Ishii (R)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan.

Ayu Fukui (A)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan.

Yuri Sakihama (Y)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan.

Shoko Kitsukawa (S)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan.

Ayami Futami (A)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan.

Takahiro Mochizuki (T)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan; Division of Medical Biochemistry, Faculty of Medicine, Tohoku Medical and Pharmaceutical University, 1-15-1, Fukumuro, Miyagino-ku, Sendai, Miyagi 983-8536, Japan.

Makoto Nagano (M)

Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan.

Jiro Toshima (J)

Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijyuku, Katsushika-ku, Tokyo 125-8585, Japan.

Fumiyoshi Abe (F)

Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, 5-10-1 Fuchinobe, Chuo-ku, Sagamihara 252-5258, Japan. Electronic address: abef@chem.aoyama.ac.jp.

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Classifications MeSH