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β-arrestin1 acts as a positive regulator that holds Gαs in a signaling-competent state, providing a unifying structural basis for sustained endosomal GPCR signaling.
Recent structural, biochemical, and physiological insights are synthesized to outline how arrestins decode regulatory inputs into signaling outcomes and how this knowledge enables the development of next-generation, structure-guided GPCR therapeutics.
Findings reveal a conserved intracellular allosteric activation mechanism across multiple class B GPCRs and identify SIM1 and its analogs as valuable chemical tools for investigating receptor-specific intracellular allosteric regulation and G protein-preferential signaling.
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