The phosphorylation-dependent activity of the α-arrestin Aly3 likely regulates various cellular processes and signaling pathways beyond the localization of the glucose transporter Ght5. α-arrestins, including Aly3, are known to act as ubiquitin ligase adaptors for specific membrane proteins, promoting their ubiquitination and subsequent endocytosis. Therefore, the phosphorylation status of Aly3 may impact the turnover and localization of other membrane proteins involved in nutrient uptake, signaling, or cellular homeostasis. Additionally, α-arrestins have been implicated in regulating endocytosis of G-protein-coupled receptors (GPCRs) and other signaling receptors, suggesting a broader role in modulating signal transduction pathways. The phosphorylation-dependent regulation of Aly3 could potentially influence the dynamics of these signaling cascades, affecting cellular responses to environmental cues and stress conditions.