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A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis
Endocytosis regulates the plasma membrane protein landscape in response to environmental cues. In yeast, the endocytosis of transporters depends on their ubiquitylation by the Nedd4-like ubiquitin ligase Rsp5, but how extracellular signals trigger this ubiquitylation is unknown. Various carbon sourc...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265958/ https://www.ncbi.nlm.nih.gov/pubmed/22249293 http://dx.doi.org/10.1083/jcb.201109113 |
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author | Becuwe, Michel Vieira, Neide Lara, David Gomes-Rezende, Jéssica Soares-Cunha, Carina Casal, Margarida Haguenauer-Tsapis, Rosine Vincent, Olivier Paiva, Sandra Léon, Sébastien |
author_facet | Becuwe, Michel Vieira, Neide Lara, David Gomes-Rezende, Jéssica Soares-Cunha, Carina Casal, Margarida Haguenauer-Tsapis, Rosine Vincent, Olivier Paiva, Sandra Léon, Sébastien |
author_sort | Becuwe, Michel |
collection | PubMed |
description | Endocytosis regulates the plasma membrane protein landscape in response to environmental cues. In yeast, the endocytosis of transporters depends on their ubiquitylation by the Nedd4-like ubiquitin ligase Rsp5, but how extracellular signals trigger this ubiquitylation is unknown. Various carbon source transporters are known to be ubiquitylated and endocytosed when glucose-starved cells are exposed to glucose. We show that this required the conserved arrestin-related protein Rod1/Art4, which was activated in response to glucose addition. Indeed, Rod1 was a direct target of the glucose signaling pathway composed of the AMPK homologue Snf1 and the PP1 phosphatase Glc7/Reg1. Glucose promoted Rod1 dephosphorylation and its subsequent release from a phospho-dependent interaction with 14-3-3 proteins. Consequently, this allowed Rod1 ubiquitylation by Rsp5, which was a prerequisite for transporter endocytosis. This paper therefore demonstrates that the arrestin-related protein Rod1 relays glucose signaling to transporter endocytosis and provides the first molecular insights into the nutrient-induced activation of an arrestin-related protein through a switch in post-translational modifications. |
format | Online Article Text |
id | pubmed-3265958 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32659582012-07-23 A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis Becuwe, Michel Vieira, Neide Lara, David Gomes-Rezende, Jéssica Soares-Cunha, Carina Casal, Margarida Haguenauer-Tsapis, Rosine Vincent, Olivier Paiva, Sandra Léon, Sébastien J Cell Biol Research Articles Endocytosis regulates the plasma membrane protein landscape in response to environmental cues. In yeast, the endocytosis of transporters depends on their ubiquitylation by the Nedd4-like ubiquitin ligase Rsp5, but how extracellular signals trigger this ubiquitylation is unknown. Various carbon source transporters are known to be ubiquitylated and endocytosed when glucose-starved cells are exposed to glucose. We show that this required the conserved arrestin-related protein Rod1/Art4, which was activated in response to glucose addition. Indeed, Rod1 was a direct target of the glucose signaling pathway composed of the AMPK homologue Snf1 and the PP1 phosphatase Glc7/Reg1. Glucose promoted Rod1 dephosphorylation and its subsequent release from a phospho-dependent interaction with 14-3-3 proteins. Consequently, this allowed Rod1 ubiquitylation by Rsp5, which was a prerequisite for transporter endocytosis. This paper therefore demonstrates that the arrestin-related protein Rod1 relays glucose signaling to transporter endocytosis and provides the first molecular insights into the nutrient-induced activation of an arrestin-related protein through a switch in post-translational modifications. The Rockefeller University Press 2012-01-23 /pmc/articles/PMC3265958/ /pubmed/22249293 http://dx.doi.org/10.1083/jcb.201109113 Text en © 2012 Becuwe et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Becuwe, Michel Vieira, Neide Lara, David Gomes-Rezende, Jéssica Soares-Cunha, Carina Casal, Margarida Haguenauer-Tsapis, Rosine Vincent, Olivier Paiva, Sandra Léon, Sébastien A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title | A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title_full | A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title_fullStr | A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title_full_unstemmed | A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title_short | A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
title_sort | molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265958/ https://www.ncbi.nlm.nih.gov/pubmed/22249293 http://dx.doi.org/10.1083/jcb.201109113 |
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