Cargando…
Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids
How cells adjust nutrient transport across their membranes is incompletely understood. Previously, we have shown that S. cerevisiae broadly re-configures the nutrient transporters at the plasma membrane in response to amino acid availability, through endocytosis of sugar- and amino acid transporters...
Autores principales: | , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7449699/ https://www.ncbi.nlm.nih.gov/pubmed/32744498 http://dx.doi.org/10.7554/eLife.58246 |
_version_ | 1783574679830659072 |
---|---|
author | Ivashov, Vasyl Zimmer, Johannes Schwabl, Sinead Kahlhofer, Jennifer Weys, Sabine Gstir, Ronald Jakschitz, Thomas Kremser, Leopold Bonn, Günther K Lindner, Herbert Huber, Lukas A Leon, Sebastien Schmidt, Oliver Teis, David |
author_facet | Ivashov, Vasyl Zimmer, Johannes Schwabl, Sinead Kahlhofer, Jennifer Weys, Sabine Gstir, Ronald Jakschitz, Thomas Kremser, Leopold Bonn, Günther K Lindner, Herbert Huber, Lukas A Leon, Sebastien Schmidt, Oliver Teis, David |
author_sort | Ivashov, Vasyl |
collection | PubMed |
description | How cells adjust nutrient transport across their membranes is incompletely understood. Previously, we have shown that S. cerevisiae broadly re-configures the nutrient transporters at the plasma membrane in response to amino acid availability, through endocytosis of sugar- and amino acid transporters (AATs) (Müller et al., 2015). A genome-wide screen now revealed that the selective endocytosis of four AATs during starvation required the α-arrestin family protein Art2/Ecm21, an adaptor for the ubiquitin ligase Rsp5, and its induction through the general amino acid control pathway. Art2 uses a basic patch to recognize C-terminal acidic sorting motifs in AATs and thereby instructs Rsp5 to ubiquitinate proximal lysine residues. When amino acids are in excess, Rsp5 instead uses TORC1-activated Art1 to detect N-terminal acidic sorting motifs within the same AATs, which initiates exclusive substrate-induced endocytosis. Thus, amino acid excess or starvation activate complementary α-arrestin-Rsp5-complexes to control selective endocytosis and adapt nutrient acquisition. |
format | Online Article Text |
id | pubmed-7449699 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-74496992020-08-27 Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids Ivashov, Vasyl Zimmer, Johannes Schwabl, Sinead Kahlhofer, Jennifer Weys, Sabine Gstir, Ronald Jakschitz, Thomas Kremser, Leopold Bonn, Günther K Lindner, Herbert Huber, Lukas A Leon, Sebastien Schmidt, Oliver Teis, David eLife Cell Biology How cells adjust nutrient transport across their membranes is incompletely understood. Previously, we have shown that S. cerevisiae broadly re-configures the nutrient transporters at the plasma membrane in response to amino acid availability, through endocytosis of sugar- and amino acid transporters (AATs) (Müller et al., 2015). A genome-wide screen now revealed that the selective endocytosis of four AATs during starvation required the α-arrestin family protein Art2/Ecm21, an adaptor for the ubiquitin ligase Rsp5, and its induction through the general amino acid control pathway. Art2 uses a basic patch to recognize C-terminal acidic sorting motifs in AATs and thereby instructs Rsp5 to ubiquitinate proximal lysine residues. When amino acids are in excess, Rsp5 instead uses TORC1-activated Art1 to detect N-terminal acidic sorting motifs within the same AATs, which initiates exclusive substrate-induced endocytosis. Thus, amino acid excess or starvation activate complementary α-arrestin-Rsp5-complexes to control selective endocytosis and adapt nutrient acquisition. eLife Sciences Publications, Ltd 2020-08-03 /pmc/articles/PMC7449699/ /pubmed/32744498 http://dx.doi.org/10.7554/eLife.58246 Text en © 2020, Ivashov et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Ivashov, Vasyl Zimmer, Johannes Schwabl, Sinead Kahlhofer, Jennifer Weys, Sabine Gstir, Ronald Jakschitz, Thomas Kremser, Leopold Bonn, Günther K Lindner, Herbert Huber, Lukas A Leon, Sebastien Schmidt, Oliver Teis, David Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title | Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title_full | Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title_fullStr | Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title_full_unstemmed | Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title_short | Complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
title_sort | complementary α-arrestin-ubiquitin ligase complexes control nutrient transporter endocytosis in response to amino acids |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7449699/ https://www.ncbi.nlm.nih.gov/pubmed/32744498 http://dx.doi.org/10.7554/eLife.58246 |
work_keys_str_mv | AT ivashovvasyl complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT zimmerjohannes complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT schwablsinead complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT kahlhoferjennifer complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT weyssabine complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT gstirronald complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT jakschitzthomas complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT kremserleopold complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT bonnguntherk complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT lindnerherbert complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT huberlukasa complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT leonsebastien complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT schmidtoliver complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids AT teisdavid complementaryaarrestinubiquitinligasecomplexescontrolnutrienttransporterendocytosisinresponsetoaminoacids |