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Open Access Publications from the University of California

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.

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.

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