Arrestins, known regulators of endocytosis, take on novel functions in nutrient-regulated endosomal recycling. Yeast α-arrestins, Aly1 and Aly2, redistribute the Gap1 permease from endosomes to the cell surface and interact with clathrin/AP-1. Aly2 is regulated by the Npr1 kinase and acts through mechanisms distinct from Aly1

Alex Apffel

Allyson F. O'Donnell

Alvarez C. E.

Andreasson C.

Annan R. B.

Ausubel F. M.

Bennett-Lovsey R. M.

Boeckstaens M.

Bonifacino J. S.

Bultynck G.

Carroll S. Y.

Chen E. J.

David G. Drubin

De Craene J. O.

Doray B.

Duncan M. C.

Edeling M. A.

Foote C.

Goldstein A. L.

Goodman O. B.

Grenson M.

Gupta R.

Hartwell L. H.

Helliwell S. B.

Hou J. C.

Huh W. K.

Johnston G. C.

Kee Y.

Kelley L. A.

Kiselev A.

Krogan N. J.

Krupnick J. G.

Laporte S. A.

Lauwers E.

Lin C. H.

Longtine M. S.

Martha S. Cyert

Nikko E.

Omura F.

Richard G. Gardner

Roberg K. J.

Schmidt A.

Shenoy S. K.

Shi H.

Soetens O.

Soussi-Boudekou S.

Ungar D.

Urbanowski J. L.

Valdivia R. H.

Vida T. A.

Volland C.

von der Haar T.

Yeung B. G.

Zheng X. F.

Zhu H.

English

PubMed

Extracellular signals regulate trafficking events to reorganize proteins at the plasma membrane (PM); however, few effectors of this regulation have been identified. β-Arrestins relay signaling cues to the trafficking machinery by controlling agonist-stimulated endocytosis of G-protein–coupled receptors. In contrast, we show that yeast α-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 α-arrestins with clathrin and clathrin adaptor proteins (AP) and show that Aly1 and Aly2 interact directly with the γ-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. 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 α-arrestins coordinate signaling events with protein trafficking.</jats:p

Crossref

Molecular Biology of the Cell

α-Arrestins Aly1 and Aly2 Regulate Intracellular Trafficking in Response to Nutrient Signaling

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http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2954120

α-Arrestins Aly1 and Aly2 Regulate Intracellular Trafficking in Response to Nutrient Signaling

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