GNAO1 antibody
- Known as:
- GNAO1 (anti-)
- Catalog number:
- orb2460
- Product Quantity:
- 200ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- GNAO1 antibody
Related genes to: GNAO1 antibody
- Gene:
- GNAO1 NIH gene
- Name:
- G protein subunit alpha o1
- Previous symbol:
- -
- Synonyms:
- G-ALPHA-o
- Chromosome:
- 16q13
- Locus Type:
- gene with protein product
- Date approved:
- 1988-04-24
- Date modifiied:
- 2016-03-03
Related products to: GNAO1 antibody
Related articles to: GNAO1 antibody
- GNAO1-related disorder (GNAO1-RD) is ultra-rare and clinically heterogeneous. Often, children with GNAO1-RD have (severe) motor impairments, which may lead to an underestimation of their communication abilities. To help these children achieve their full potential in daily life, it is essential to understand their communicative abilities and limitations. In this study, we aimed to investigate spoken language comprehension (SLC), speech and functional communication. - Source: PubMed
Publication date: 2026/06/05
Heideman Larissa RGeytenbeek JohannaWolf Nicole IBuizer Annemieke Ivan de Pol Laura A - G protein-coupled receptors (GPCRs) enable chemical communication between cells and are involved in nearly all essential functions. They transduce signals via heterotrimeric G proteins and are regulated by internalization, a process which redirects them from the cell surface to internal compartments and enables diversified signaling through spatial reorganization. Beyond the receptor, a vast regulatory network exists to further control G-protein signaling. However, it is unclear whether these modes of G-protein regulation also impact the upstream GPCR. Here, we systematically address how G-protein cycle regulation shapes GPCR internalization and establish several key principles and mechanisms governing this process. We find that timing of G-protein activation and deactivation and changes in G-protein cycle lifetime imparted by guanine nucleotide exchange factors, activators of G-protein signaling, and regulators of G-protein signaling can alter internalization outcomes. Furthermore, we determine how the activity and balance of discrete G-protein components interact with the G protein-coupled receptor kinase system to influence GPCR spatial distribution. Finally, we uncover that disease-associated variants of the most abundant G protein in the brain, GαoA, affect the regulatory network that drives GPCR internalization. Altogether, this study reveals that GPCR internalization is not a fixed receptor property but is dynamically governed by receptor-G-protein activation order, cycle lifetime, and the balance of Gα and Gβγ availability. As such, alterations in receptor internalization dynamics may contribute to the complex disease phenotypes associated with dysregulated G-protein networks. - Source: PubMed
Publication date: 2026/06/09
Rowe Jacob BPandey ShubhiMayer Ryan ALudlam W GrantDrube JuliaInoue AsukaHoffmann CarstenMartemyanov Kirill A - : Pathogenic variants in , encoding the inhibitory G protein subunit Gαo, cause severe neurodevelopmental disorders that remain largely refractory to pharmacological treatments. Gαo transduces inhibitory signals downstream of multiple G protein-coupled receptors (GPCRs) involved in motor control. Here, we used gene-edited models carrying variants, the ortholog of , to investigate GPCR contributions to Gαo-dependent locomotor phenotypes. : We combined pharmacological screening of dopamine- and cannabinoid-targeting ligands in mutants with structural analysis of ligand-binding pocket conservation and genetic perturbation of receptor function using RNAi and knockout approaches. : Pharmacological modulation of GPCR signaling produced non-linear and context-dependent effects. Compounds predicted to further increase excitability may instead promote phenotypic improvement, consistent with compensatory network rebalancing. Structural analyses revealed substantial divergence in ligand-binding pocket conservation for several GPCR-ligand pairs, suggesting that altered binding affinity and selectivity may also contribute to the observed phenotypic outcome. Pharmacological experiments performed in GPCR-depleted mutants allowed for the correlation of structural findings with functional effects for selected receptor-ligand pairs. Finally, genetic reduction in GPCRs coupled to stimulatory G proteins ameliorated hyperactive locomotion in mutants, whereas reduction in GPCRs coupled to inhibitory G proteins is largely insufficient to induce or exacerbate locomotor defects. : Our findings identify excessive excitatory GPCR input as a key modulator of motor dysfunction in the context of impaired Gαo signaling. They also show that structural conservation is a necessary but not sufficient condition to predict functional responses. Overall, this study establishes as a suitable platform to dissect GPCR-mediated signaling and highlights the value of integrating pharmacological and genetic approaches to guide target selection in -related disorders. - Source: PubMed
Publication date: 2026/05/18
Di Rocco MartinaDi Rienzo LorenzoFollo Francesca CarmenD'Alessandro ManuelaGalosi SerenaPannone LucaVenanzi SerenellaDi Schiavi EliaMartire AlbertoBessereau Jean-LouisLeuzzi VincenzoMilanetti EdoardoMartinelli Simone - Growth hormone (GH) stimulation tests have limited reliability and may lead to false-positive results. - Source: PubMed
Publication date: 2026/05/07
Plachy LukasDusatkova PetraKavciak LukasAmaratunga Shenali AnneSlavenko MatveiDrabova JanaMaratova KlaraNeuman VitObermannova BarboraKolouskova StanislavaSnajderova MartaSumnik ZdenekLebl JanPruhova Stepanka - GNAO1-related neurodevelopmental disorders are caused by mutations in the GNAO1 gene encoding the major neuronal G protein, Gαo. GNAO1 encephalopathies manifest in a range of symptoms, including epilepsy, movement disorder, hypotonia, and developmental delay, affecting >400 patients worldwide to date. A growth in the number of diagnosed cases is expected due to the wider availability of whole genome sequencing. One of the most recurrent pathogenic variants causing GNAO1 encephalopathy is an intronic mutation c.724-8G>A, which results in an in-frame insertion of two amino acid residues, Pro-Gln, after Thr241: Gαo[T241_N242insPQ]. We previously performed in-depth profiling of Gαo[insPQ] using structural, biochemical, and cellular studies. Compared with the wild-type protein, Gαo[insPQ] exhibits faster GTP binding and decreased hydrolysis. Importantly, Gαo[insPQ] is deficient in interacting with regulator of G protein signaling (RGS), GTPase-activating proteins that deactivate Gαo. These defects render Gαo[insPQ] a constitutively active mutant loaded with GTP in the G protein signaling. Patients harboring Gαo[insPQ] variant are in urgent need of novel therapy as they are refractory to available medications. In the present study, we performed a high-throughput screening to find molecules that might suppress the constitutive GTP loading by Gαo[insPQ]. We used a high-diversity chemical library of 54080 compounds, identifying a novel compound, N-[5-(2-methylpropyl)-1,3,4-thiadiazol-2-yl]-1H-1,2,3-benzotriazole-5-carboxamide, that decreases the GTP binding rate of Gαo, likely acting as a competitive inhibitor with higher selectivity to the pathogenic protein. This small-molecule inhibitor of Gαo opens new opportunities to drug discovery towards Gαo-dependent pathologies. - Source: PubMed
Larasati Yonika AKoval AlexeyKatanaev Vladimir L