M. von Zastrow

This paper shows that VIPR1 can generate endosomal cAMP signals without β-arrestin, revealing β-arrestin's role in shaping the spatiotemporal profile of GPCR signaling.

The paper uses a CRISPR interference screen with a trafficking biosensor to identify genes regulating opioid receptor trafficking, finding RME-8 as a novel regulator.

This study identifies two distinct GPCR-triggered endocytic modes in β-arrestins, each with different signaling outcomes and receptor-specific activation.

This study identifies membrane phosphoinositides as regulators of GPCR-arrestin complex dynamics, showing they stabilize complexes and enable temporal control of receptor signaling and recycling.

The paper shows that endosomal cAMP production leads to distinct phosphoproteomic changes compared to plasma membrane cAMP, with a strong bias toward dephosphorylation by PP2A-B56{delta}.

The paper develops a CRISPR interference screen to identify regulators of GPCR/cAMP signaling, identifying 45 strong and 50 weaker regulators, and validates seven novel mediators.

This study identifies two macrocyclic peptides that selectively modulate active and inactive states of Gs, offering a new approach for developing state-dependent GTPase inhibitors.

This study shows AC9 traffics from the plasma membrane to endosomes via Gs, unlike AC1, and contributes to cAMP production from endosomes.

The paper develops a cell-based assay to study agonist-selective recruitment of engineered protein probes and GRK2 by opioid receptors in living cells, showing differential recruitment by distinct opioid ligands.