Asuka Inoue

The paper determines structural states of the US28-Gq complex to elucidate a stepwise G protein activation mechanism.

The paper studies the behavior of human RTKs using single-molecule imaging and finds that molecular behavior correlates with cell growth regulation.

This paper develops a NanoBiT-based platform to systematically study multiple layers of GPCR signaling in living cells.

This study shows Gβγ enhances PLCβ3 activation by reorienting its catalytic site, working with Gq to increase PI(4,5)P2 hydrolysis and Ca2+ release.

This paper identifies naturally-encoded signaling bias at C5aR1 and C5aR2 receptors through structural and functional analyses, revealing molecular mechanisms underlying biased signaling in GPCRs.

This study predicts 3D structures of human GPCR-G protein complexes using AlphaFold3 and uses machine learning to predict coupling potency, revealing new signaling mechanisms and coupling preferences across GPCR subtypes.

This study investigates how GPCRs regulate G protein activity on endosomes using conformational biosensors, finding that endocytosis is required for active Gs production on endosomes.

The paper challenges the conventional view of GPCR internalization by showing multiple pathways regulate receptor internalization, with specific findings on the GLP-1R's mechanism.

This study uses single-molecule imaging to show that opioid receptors form transient homodimers, with distinct functional effects on signaling and internalization depending on the receptor subtype.

This study investigates the structural dynamics of the human KOR-Gi signaling complex with G-protein-biased and balanced agonists, identifying key residues involved in signaling bias.

This study designs allosteric modulators that alter GPCR G protein subtype selectivity by targeting the receptor-transducer interface, demonstrating predictable mechanisms for rational drug design.

The paper investigates how amylin receptor subunit interactions are modulated by agonists and how these interactions influence cAMP signaling.

This study identifies non-canonical internalization mechanisms for mGlu receptors, showing some require neither GRKs nor beta-arrestins for agonist-induced internalization.

This study reveals that membrane phosphoinositides allosterically regulate β-arrestin dynamics, enabling engagement with minimally phosphorylated GPCRs.

Antimuscarinic drugs act as β-arrestin-biased agonists via casein kinase 2 activation to promote ERK1/2 phosphorylation and neurite outgrowth.

This study shows that GPCRs regain G protein signaling without endocytosis by sorting into an AP2-positive plasma membrane compartment, regulated by PI(4,5)P2 and beta-arrestins.

This study identifies structural features determining G protein coupling specificity at a class A GPCR using a Gi-biased agonist.

The paper characterizes a rare GHSR variant, L149P, revealing novel roles of intracellular loop-2 in GPCR biased signaling, lipid modulation, and trafficking through experimental and computational methods.

This study investigates how ETB couples to different G proteins, finding that it interacts with Gi and Gq but not Gs, with specific regions influencing these interactions.

This study reports the cryo-EM structure of the QRFP-GPR103-Gq complex, revealing unique binding mechanisms and insights into RF-amide peptide recognition.

The paper determines the cryo-EM structure of activated S1PR4, revealing mechanisms of ligand recognition and Gi coupling to aid in developing safer S1PR4 agonists.

The paper develops a four-color single-molecule imaging system using fluorescent HiBiT peptides to track GPCR dynamics and interactions in living cells.

This study identifies G protein-biased LPAR1 agonism as a mechanism underlying the antidepressant effects of TCAs like amitriptyline, distinguishing them from SSRIs.

The paper analyzes GPCR-G-protein complexes to identify structural determinants of G-protein coupling selectivity, revealing differences in contact patterns and stability between Gs and Gi/o complexes.

The paper identifies m6A as an endogenous ligand for the A3 adenosine receptor, showing it has higher affinity than unmodified adenosine and plays a role in type I allergy.

The paper presents a cryo-EM structure of the human PAC1 receptor bound to PACAP and an engineered Gs heterotrimer, revealing functional differences in the ECD between PAC1R and GLP1R.

The paper reports X-ray structures of the human ETB receptor bound to agonists, revealing molecular mechanisms of activation and partial agonism.