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The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis

Yeast cells have a remarkable ability to adapt to nutritional changes in their environment. During adaptation, nutrient-signaling pathways drive the selective endocytosis of nutrient transporters present at the cell surface. A current challenge is to understand the mechanistic basis of this regulati...

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Autores principales: Hovsepian, Junie, Albanèse, Véronique, Becuwe, Michel, Ivashov, Vasyl, Teis, David, Léon, Sébastien
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5921569/
https://www.ncbi.nlm.nih.gov/pubmed/29514933
http://dx.doi.org/10.1091/mbc.E17-07-0466
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author Hovsepian, Junie
Albanèse, Véronique
Becuwe, Michel
Ivashov, Vasyl
Teis, David
Léon, Sébastien
author_facet Hovsepian, Junie
Albanèse, Véronique
Becuwe, Michel
Ivashov, Vasyl
Teis, David
Léon, Sébastien
author_sort Hovsepian, Junie
collection PubMed
description Yeast cells have a remarkable ability to adapt to nutritional changes in their environment. During adaptation, nutrient-signaling pathways drive the selective endocytosis of nutrient transporters present at the cell surface. A current challenge is to understand the mechanistic basis of this regulation. Transporter endocytosis is triggered by their ubiquitylation, which involves the ubiquitin ligase Rsp5 and its adaptors of the arrestin-related family (ART). This step is highly regulated by nutrient availability. For instance, the monocarboxylate transporter Jen1 is ubiquitylated, endocytosed, and degraded upon exposure to glucose. The ART protein Rod1 is required for this overall process; yet Rod1 rather controls Jen1 trafficking later in the endocytic pathway and is almost dispensable for Jen1 internalization. Thus, how glucose triggers Jen1 internalization remains unclear. We report that another ART named Bul1, but not its paralogue Bul2, contributes to Jen1 internalization. Bul1 responds to glucose availability, and preferentially acts at the plasma membrane for Jen1 internalization. Thus, multiple ARTs can act sequentially along the endocytic pathway to control transporter homeostasis. Moreover, Bul1 is in charge of Jen1 endocytosis after cycloheximide treatment, suggesting that the functional redundancy of ARTs may be explained by their ability to interact with multiple cargoes in various conditions.
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spelling pubmed-59215692018-07-16 The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis Hovsepian, Junie Albanèse, Véronique Becuwe, Michel Ivashov, Vasyl Teis, David Léon, Sébastien Mol Biol Cell Brief Reports Yeast cells have a remarkable ability to adapt to nutritional changes in their environment. During adaptation, nutrient-signaling pathways drive the selective endocytosis of nutrient transporters present at the cell surface. A current challenge is to understand the mechanistic basis of this regulation. Transporter endocytosis is triggered by their ubiquitylation, which involves the ubiquitin ligase Rsp5 and its adaptors of the arrestin-related family (ART). This step is highly regulated by nutrient availability. For instance, the monocarboxylate transporter Jen1 is ubiquitylated, endocytosed, and degraded upon exposure to glucose. The ART protein Rod1 is required for this overall process; yet Rod1 rather controls Jen1 trafficking later in the endocytic pathway and is almost dispensable for Jen1 internalization. Thus, how glucose triggers Jen1 internalization remains unclear. We report that another ART named Bul1, but not its paralogue Bul2, contributes to Jen1 internalization. Bul1 responds to glucose availability, and preferentially acts at the plasma membrane for Jen1 internalization. Thus, multiple ARTs can act sequentially along the endocytic pathway to control transporter homeostasis. Moreover, Bul1 is in charge of Jen1 endocytosis after cycloheximide treatment, suggesting that the functional redundancy of ARTs may be explained by their ability to interact with multiple cargoes in various conditions. The American Society for Cell Biology 2018-05-01 /pmc/articles/PMC5921569/ /pubmed/29514933 http://dx.doi.org/10.1091/mbc.E17-07-0466 Text en © 2018 Hovsepian, Albanèse, et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0/ This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
spellingShingle Brief Reports
Hovsepian, Junie
Albanèse, Véronique
Becuwe, Michel
Ivashov, Vasyl
Teis, David
Léon, Sébastien
The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title_full The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title_fullStr The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title_full_unstemmed The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title_short The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis
title_sort yeast arrestin-related protein bul1 is a novel actor of glucose-induced endocytosis
topic Brief Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5921569/
https://www.ncbi.nlm.nih.gov/pubmed/29514933
http://dx.doi.org/10.1091/mbc.E17-07-0466
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