Proteins BAI3, Human
- Known as:
- Proteins BAI3, Human
- Catalog number:
- C431
- Product Quantity:
- 10μg
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Proteins BAI3 Human
Related genes to: Proteins BAI3, Human
- Gene:
- ADGRB3 NIH gene
- Name:
- adhesion G protein-coupled receptor B3
- Previous symbol:
- BAI3
- Synonyms:
- KIAA0550
- Chromosome:
- 6q12-q13
- Locus Type:
- gene with protein product
- Date approved:
- 1998-06-05
- Date modifiied:
- 2018-02-13
Related products to: Proteins BAI3, Human
Related articles to: Proteins BAI3, Human
- The GAIN domain is a hallmark of adhesion G protein-coupled receptors (aGPCRs), as this extracellular domain contains an integral agonistic sequence (Stachel) that activates the receptor by binding to its 7-transmembrane helix (7TM) domain. Many aGPCRs undergo autoproteolytic cleavage at the GPCR proteolysis site (GPS), which has a canonical H-X-S/T sequence motif located within the GPCR autoproteolysis-inducing (GAIN) domain. Here we present the crystal structure of the Hormone Receptor (HormR) and GAIN domains of ADGRB2/BAI2. The protein was not cleaved at the GPS, despite possessing an HLS sequence. Through structural comparisons and molecular dynamics (MD) simulations, we identify determinants that contribute to autoproteolytic activity beyond the H-X-S/T motif. Specifically, we highlight a T-shaped π-π interaction between the histidine base of the H-X-S/T motif and a phenylalanine residue that is highly conserved in cleavage-competent aGPCRs. This interaction is critical for properly positioning the imidazole group of the histidine to deprotonate the alcohol nucleophile. Disruption of this interaction reduces autoproteolytic activity in the ADGRL1 and introduction of the phenylalanine restores cleavage competence in the otherwise non-cleavable ADGRB3 upon expression in HEK293 cells. In addition, the poorly conserved and flexible flap regions flanking the GPS also contribute to full autocleavage activity. - Source: PubMed
Publication date: 2026/04/06
Pohl FabianSeufert FlorianChung Yin KwanSchick RobinKieslich BjörnSchöneberg TorstenLangenhan TobiasHildebrand Peter WSträter Norbert - Acetylcholinesterase (AChE) is a cholinergic enzyme that hydrolyzes the neurotransmitter acetylcholine (ACh). Dysregulated AChE activity is closely linked to neurodegenerative diseases and cancer. Current chemical probes for AChE detection mostly rely on single-modality fluorescence readouts, limiting their utility. Herein, we developed a set of activity-based multimodal probes, termed , , , and , which combine the complementary strengths of near-infrared fluorescence (NIRF) imaging, photoacoustic (PA) detection, and proteome profiling. These probes offer a comprehensive toolset for deciphering the AChE code in complex biological systems. // enable continuous monitoring of AChE activity via NIRF/PA detection, while represents the first trimodal probe for simultaneous NIRF/PA imaging and proteome profiling in live systems. Notably, the usage of and (1) highlighted the superior capability of PA imaging for deep-tissue studies in live animals, (2) revealed significantly elevated AChE activity in microglia compared to astrocytes in the depressive brain, and (3) identified a functional link between AChE and adhesion G protein-coupled receptor B2 and B3 (ADGRB2 and ADGRB3) in both cellular and murine models of depression. Our study not only provides powerful molecular tools for studying cholinergic systems but also reveals novel therapeutic targets for depression intervention. - Source: PubMed
Publication date: 2026/01/21
Xiang JingWang HaoLi LonghuiYang XuelinXu GuangyuYan JiaqianLi TaoShi ZhengyangXu ChunfaWang RuiTu QidongWang MiaomiaoXie Yusheng - Despite notable progress in psychiatric genomics, there are no validated blood-based biomarkers for psychosis. Previous studies have failed to establish a link between schizophrenia polygenic scores (PGS) and blood protein levels. We aimed to identify associations between schizophrenia PGS and blood-based proteins, and to determine whether levels of 2077 proteins differ in individuals with psychosis. We analysed proteomic and genomic data from 47,969 participants in the UK Biobank. Association analyses in the 47,678 participants without psychosis (mean age 57.1 years, standard deviation 8.1 years; 54% female) identified nominal associations (p < 0.05) of schizophrenia PGS with 102 proteins. Four of these (TMPRSS15, ADGRB3, CEACAM21, and KLK1) met the false discovery rate (FDR) threshold of < 0.05. We investigated the association of these four proteins with psychosis in a matched case-control sample (283 cases, 849 controls, mean age 56.9 years, standard deviation 8.4 years; 48% female). In individuals with psychosis, we observed significantly lower levels of KLK1, even after adjusting for potential confounders (effect size -0.25, SE 0.09, FDR 0.049). This direction of effect was opposite to that observed in the primary analysis of individuals without psychosis (effect size 324.67, SE 48.32, FDR 3.85 × 10). The effect of antipsychotic medication did not explain this difference. This protein should be taken forward for further study and validation to investigate its potential as a psychosis biomarker. - Source: PubMed
Publication date: 2026/01/14
Kendall Kimberley MLegge Sophie EFenner EilidhHolmans PeterWalters James Tr - Cell adhesion molecules (CAMs) are pivotal in establishing and maintaining synaptic connectivity. Emerging evidence indicates that some secreted factors within the synaptic cleft, including C1q-like proteins (C1qls), play a crucial role in bridging pre- and post-synapses by connecting the bilateral CAMs. However, the mechanisms of those secreted factors in synapse assembly remain incomplete. Here, we explore C1ql-mediated synaptic connectivity, focusing on the assembly of C1ql1 and its postsynaptic receptor brain-specific angiogenesis inhibitor 3 (BAI3, also called ADGRB3). Our biochemical, structural, and computational analyses reveal that the trimeric globular C1q (gC1q) domain of C1ql1 undergoes a calcium-modulated domain-swapping event to form a hexamer. Cryo-EM study manifests the stabilizing role of calcium ions on the C1ql1_gC1q hexamer in complex with the extended CUB domain of BAI3. Using the gC1q hexamer, full-length C1ql1 further assembles into linear clusters, possibly providing a scaffold to accumulate BAI3 receptors on the plasma membrane. Our cellular and in vivo studies support a role for the gC1q-mediated dynamic assembly of C1ql1 in receptor accumulation and synapse maintenance. Collectively, our findings provide a plausible mechanism of secreted factor-mediated synaptic connectivity, driven by the calcium-modulated assembly of C1qls and their interactions with CAMs. - Source: PubMed
Publication date: 2025/12/10
Liao LiangyuHan YingNiu FengfengWang YingjieLu YangXu ShunZhu HoumingLin LeishuXiao JinmanTou Hoi InGao JialiZhang BoWei Zhiyi - The Licha Black pig (LC) is a nationally protected Chinese indigenous breed known for its superior meat quality and strong environmental adaptability. However, its population has declined rapidly due to extensive crossbreeding with commercial lines. Understanding the genetic basis of its economically important traits is crucial for conservation and genomic improvement. - Source: PubMed
Publication date: 2025/12/03
Liu JiajiaTian ZheYu MubinLi WenwenLv PengchengWang TaoTian YuZhang ShuerWang JunjieShen Wei