J. Selent

Multiple triggers converge to preferential effector coupling in the CB2R through a complex allosteric communication network

The paper investigates how multiple triggers on an allosteric communication network influence preferential coupling of the CB2R to Gi2 over β-arrestin1, revealing insights into GPCR signaling mechanisms.

Molecular insights into atypical modes of beta-arrestin interaction with seven transmembrane receptors

This study presents cryo-EM structures and experimental data revealing how beta-arrestins interact with GPCRs, particularly those with phosphorylation in the third intracellular loop and intrinsically biased receptors.

Phosphorylation barcodes direct biased chemokine signaling at CXCR3

The paper shows that CXCR3 chemokines use different phosphorylation barcodes to activate distinct signaling pathways, leading to varied physiological outcomes.

Single-molecule analysis of receptor-beta-arrestin interactions in living cells

This study uses single-molecule microscopy and simulations to show that beta-arrestin inserts into the lipid bilayer and interacts with receptors through lateral diffusion, challenging existing models of its function.

Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody

This paper shows that a synthetic intrabody enhances β-arrestin endosomal trafficking and ERK1/2 activation in a GPCR mutant by promoting an active-like conformation.

Impact of membrane lipid polyunsaturation on dopamine D2 receptor ligand binding and signaling

This study shows that n-3 PUFAs enhance D2R ligand binding and signaling, suggesting they act as allosteric modulators of the receptor.

Entrectinib - a SARS-CoV-2 inhibitor in Human Lung Tissue (HLT) cells

This study identifies entrectinib as a potential antiviral drug against SARS-CoV-2 using drug repurposing, virtual screening, and in vitro assays in Human Lung Tissue cells.

Conformational sensors and domain-swapping reveal structural and functional differences between β-arrestin isoforms

The paper identifies structural differences between β-arrestin isoforms using conformational sensors and domain-swapping, linking these differences to their distinct functional outcomes in GPCR signaling.

Genetically encoded intrabody sensors illuminate structural and functional diversity in GPCR-β-arrestin complexes

This study uses genetically encoded intrabody sensors to reveal structural and functional diversity in GPCR-β-arrestin complexes, showing distinct functional outcomes across different receptors.