A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis. - Archive ouverte HAL Access content directly
Journal Articles Journal of Cell Biology Year : 2012

A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis.

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Abstract

Endocytosis regulates the plasma membrane protein landscape in response to environmental cues. In yeast, the endocytosis of transporters depends on their ubiquitylation by the Nedd4-like ubiquitin ligase Rsp5, but how extracellular signals trigger this ubiquitylation is unknown. Various carbon source transporters are known to be ubiquitylated and endocytosed when glucose-starved cells are exposed to glucose. We show that this required the conserved arrestin-related protein Rod1/Art4, which was activated in response to glucose addition. Indeed, Rod1 was a direct target of the glucose signaling pathway composed of the AMPK homologue Snf1 and the PP1 phosphatase Glc7/Reg1. Glucose promoted Rod1 dephosphorylation and its subsequent release from a phospho-dependent interaction with 14-3-3 proteins. Consequently, this allowed Rod1 ubiquitylation by Rsp5, which was a prerequisite for transporter endocytosis. This paper therefore demonstrates that the arrestin-related protein Rod1 relays glucose signaling to transporter endocytosis and provides the first molecular insights into the nutrient-induced activation of an arrestin-related protein through a switch in post-translational modifications.

Dates and versions

hal-00665246 , version 1 (01-02-2012)

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Michel Becuwe, Neide Vieira, David Lara, Jéssica Gomes-Rezende, Carina Soares-Cunha, et al.. A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis.. Journal of Cell Biology, 2012, 196 (2), pp.247-59. ⟨10.1083/jcb.201109113⟩. ⟨hal-00665246⟩
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