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Unresolved aspects of ß-arrestin/GPCR interactions and phosphorylation motifs

Characterize the phosphorylation motifs and other determinants that underlie ß-arrestin interactions with G protein–coupled receptors, resolving the outstanding ambiguities regarding how these features govern ß-arrestin recognition and complex formation.

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Background

Using ARIP across multiple receptors, the authors observe variable inhibitory effects, discuss potential roles for phosphorylation motifs (e.g., PxPP), and note minimal C-terminal sequence identity among receptors.

They conclude that key aspects of ß-arrestin/receptor interactions—including which phosphorylation patterns and motifs drive binding and functional outcomes—are still not fully defined.

References

Perhaps most critically, many aspects of the ß-arrestin/receptor interaction and the phosphorylation motifs underlying it remain unresolved.

— A lipidated peptide derived from the C-terminal tail of the vasopressin 2 receptor shows promise as a new $β$-arrestin inhibitor (2411.07258 - Brouillette et al., 2 Nov 2024) in Section 3.2