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O'Donnell AF, et al.  (2010) {alpha}-Arrestins Aly1 and Aly2 Regulate Intracellular Trafficking in Response to Nutrient Signaling. Mol Biol Cell 21(20):3552-66

Abstract: Monitoring Editor: David G. Drubin Extracellular signals regulate trafficking events to reorganize proteins at the plasma membrane (PM), however few effectors of this regulation have been identified. beta-arrestins relay signaling cues to the trafficking machinery by controlling agonist-stimulated endocytosis of G-protein coupled receptors. In contrast, we show that yeast alpha-arrestins, Aly1 and Aly2, control intracellular sorting of Gap1, the general amino acid permease, in response to nutrients. These studies are the first to demonstrate association of alpha-arrestins with clathrin and clathrin adaptor proteins (AP), and show that Aly1 and Aly2 interact directly with the gamma subunit of AP-1, Apl4. Aly2-dependent trafficking of Gap1 requires AP-1, which mediates endosome-to-Golgi transport, and the nutrient-regulated kinase, Npr1, which phosphorylates Aly2. During nitrogen starvation, Npr1 phosphorylation of Aly2 may stimulate Gap1 incorporation into AP-1/clathrin-coated vesicles to promote Gap1 trafficking from endosomes to the trans-Golgi network (TGN). Ultimately, increased Aly1-/Aly2-mediated recycling of Gap1 from endosomes results in higher Gap1 levels within cells and at the PM by diverting Gap away from trafficking pathways that lead to vacuolar degradation. This work defines a new role for arrestins in membrane trafficking and offers insight into how alpha-arrestins coordinate signaling events with protein trafficking.

Status: Published Type: Journal Article PubMed ID: 20739461

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ALY1 ALY2 APL2 APL4 BUL1 BUL2 GAP1 LST4 NPR1
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