A calcineurin-dependent switch controls the trafficking function of α-arrestin Aly1/Art6
- Author(s): O'Donnell, AF
- Huang, L
- Thorner, J
- Cyert, MS
- et al.
Published Web Locationhttps://doi.org/10.1074/jbc.M113.478511
Background: In response to nutrient signals, α-arrestins selectively regulate trafficking of membrane transporters. Results: Aly1 is a substrate of the phosphatase calcineurin, and dephosphorylation triggers Aly1-dependent internalization of the permease Dip5. Conclusion: Endocytic function of α-arrestins is stimulated by removal of inhibitory phosphorylation. Significance: These insights define a molecular mechanism controlling the function of an α-arrestin in endocytosis, which is critical for cellular adaptation. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
Many UC-authored scholarly publications are freely available on this site because of the UC Academic Senate's Open Access Policy. Let us know how this access is important for you.