D. Arac

Structural analysis and conformational dynamics of a holo-adhesion GPCR reveal interplay between extracellular and transmembrane domains

This study uses cryo-EM and single-molecule FRET to show conformational coupling between the extracellular and transmembrane domains of an aGPCR, revealing how ECR dynamics influence receptor function.

The far extracellular CUB domain of the adhesion GPCR ADGRG6/GPR126 is a key regulator of receptor signaling

This study investigates how the CUB domain of ADGRG6 regulates receptor signaling by modulating conformational dynamics of the extracellular region.

Structural basis for regulation of CELSR1 by a compact module in its extracellular region

This study determines the structure of the CELSR1 extracellular region and shows how specific domains form a compact module to regulate cellular adhesion.

Structural basis and functional roles for Toll-like receptor binding to Latrophilin adhesion-GPCR in embryo development

This study identifies TOL-1 as a ligand for LAT-1 in C. elegans, showing their interaction is essential for embryonic development.

The adhesion GPCRs CELSR1-3 and LPHN3 engage G proteins via distinct activation mechanisms

This study investigates how different adhesion GPCRs, CELSR1-3 and LPHN3, engage G proteins through distinct activation mechanisms, revealing that cleavage is not universal among aGPCRs.

Isoform- and ligand-specific modulation of the adhesion GPCR ADGRL3/Latrophilin3 by a synthetic binder

This study develops an antibody that specifically modulates ADGRL3 function without affecting ADGRL1, demonstrating isoform- and ligand-specific aGPCR modulation.

Structure of the teneurin-latrophilin complex: Alternative splicing controls synapse specificity by a novel mechanism

The paper reports the cryo-EM structure of the Tenm2-Lphn3 complex and shows how alternative splicing regulates synapse specificity by affecting access to the Lphn-binding site.

Structural basis for adhesion G protein-coupled receptor Gpr126 function

This study determines the structure of the zebrafish Gpr126 ECR, revealing a closed conformation stabilized by alternative splicing and a calcium-binding site, and shows how these features regulate receptor function.