Journal
ELIFE
Volume 9, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.58246
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Funding
- European Molecular Biology Organization [ALTF 642-2012, EMBOCOFUND2010, GA-2010-267146]
- Tiroler Wissenschaftsfonds
- Austrian Science Fund [FWF-Y444-B12, P30263, P29583]
- Agence Nationale de la Recherche [ANR-16-CE13-0002-01]
- MCBO [W1101-B18]
- Austrian Science Fund (FWF) [P29583, P30263] Funding Source: Austrian Science Fund (FWF)
- Agence Nationale de la Recherche (ANR) [ANR-16-CE13-0002] Funding Source: Agence Nationale de la Recherche (ANR)
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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) (Muller et al., 2015). A genome-wide screen now revealed that the selective endocytosis of four AATs during starvation required the alpha-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 alpha-arrestin-Rsp5-complexes to control selective endocytosis and adapt nutrient acquisition.
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