Receptor Mechanisms and Signaling

The paper investigates how splice variants of GIPR modulate cAMP and β-arrestin signaling independently of ligand binding.

The paper evaluates GRK antibodies for western blot specificity and introduces a method to compare protein abundance using suitable antibodies.

The paper reports cryo-EM structures of GALR1-Go and GALR2-Gq complexes with galanin and spexin, revealing structural determinants for G protein selectivity and the role of zinc as a negative allosteric regulator.

The paper develops a stochastic model of GPCR function in inflamed environments and validates it with experimental data, showing that low pH has a greater impact on GPCR behavior than radicals.

The paper uses sequence coevolutionary analysis and structural contacts to reveal distinct residue interactions in GPCR classes A and B, providing insights for drug design.

The paper identifies a splice variant of the GHRHR receptor that mediates constitutive signal bias towards β-arrestin recruitment, impacting downstream signaling pathways in prostate cancer cells.

The paper introduces ConDock, a method for predicting ligand binding sites in GPCRs using docking and sequence conservation, showing improved accuracy over traditional methods.

The paper shows that endogenous mu- and delta-opioid receptors in cholinergic interneurons function independently despite co-expression.

The paper reports high-resolution structures of MC4R with agonists and reveals insights into ligand recognition and activation mechanisms.

The paper shows that cell-to-cell variations in V2R subcellular localization are independent of expression levels and influenced by cell-specific environments.

The paper reports cryo-EM structures of LHCGR in different activation states, revealing a push and pull mechanism of receptor activation and the role of an allosteric agonist.

This study determines cryo-EM structures of dual and triple agonists bound to GIPR, GLP-1R, and GCGR to elucidate their superior efficacy over monoagonists in glucose homeostasis.

This work develops an artificial bionic receptor that transduces biological signals across membranes using chemical tools, mimicking natural receptors' function.

The paper reports the cryo-EM structure of the human GIPR complexed with GIP and a Gs heterotrimer, revealing how GIP is recognized and activates the receptor.

The paper reports cryo-EM structures of GLP-1R with ago-allosteric modulators, revealing their mechanism of action and providing insights for therapeutic design.

This paper introduces a functional GFP-tagged Go protein in C. elegans to enable biochemical and cell biological studies of Go signaling.

The paper develops multicolor sensors to directly measure DRD1 and DRD2 receptor crosstalk in a heterodimer and finds differential inhibition of activation by phasic and tonic dopamine levels.

The paper uses molecular dynamics simulations to propose a mechanism for GPCR activation involving correlated motions of conserved polar motifs.

This study identifies subtype-specific differences in transmembrane domain interactions that influence metabotropic glutamate receptor activation.

The paper investigates how opioid ligands selectively activate G protein over β-arrestin pathways in the μ-opioid receptor using a combination of experimental and computational methods.

This study shows that over-expressing RGS9-2 in HEK-293T cells reduces the inhibitory effect of the H3R agonist on cAMP formation, suggesting RGS9-2 modulates H3R signaling.

The paper reports the structures of D1R-Gs complex bound to dopamine and LY3154207, revealing mechanisms of dopamine recognition and allosteric modulation for drug discovery.

The paper reports cryo-EM structures of a GPCR-G protein complex in lipid nanodiscs, revealing structural insights into G protein activation without stabilizing agents.

The paper analyzes variability in cryo-EM datasets of GPCR-G-protein complexes to identify common movements across different receptor-G-protein systems.

The paper characterizes the structure and function of AstR-C in T.pit, identifying Q2716.55 as critical for G protein-dependent activation.

This study identifies an anti-GPR56 monoclonal antibody that enhances Src-Fak signaling and cell adhesion through a novel extracellular domain-dependent mechanism.

The paper uses super-resolution fluorescence imaging to reveal periodic CB1 receptor clusters in neurons and their interaction with the MPS.

This paper introduces a new Rosetta protocol for modeling GPCRs with improved accuracy, enabling modeling of nearly 90% of the GPCR family using low-identity templates.

This study uses deep mutational scanning to analyze GPCR variants, identifying key residues for signaling and function across multiple GPCR classes.

The paper uses molecular dynamics simulations to study how Gi inhibits AC5 and how ATP regulates this inhibition and stimulation.