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Significance Gαs protein is classically known as a signaling component of cell surface G protein-coupled receptor transduction pathways. However, Gαs has also been localized on endosomes, where it plays a role in receptor sorting to lysosomes. How Gαs regulates this trafficking step is unclear. Although Gαs structure has been known for years, we found a motif in Gαs that allows its interaction with ubiquitin, a key signal for cargo sorting to the lysosomal pathway. We show that disrupting the ubiquitin-interacting motif (UIM) in Gαs impairs its interaction with components of the endosomal sorting machinery and the lysosomal degradation of epidermal growth factor receptor. This study provides molecular insights on the mechanism by which Gαs is involved in this noncanonical function.

Gα s protein binds ubiquitin to regulate epidermal growth factor receptor endosomal sorting

Gα _s protein binds ubiquitin to regulate epidermal growth factor receptor endosomal sorting