Adhesion G protein-coupled receptor B1 (ADGRB1 (BAI1))

Adhesion G protein-coupled receptor B1 (ADGRB1) is a large cell surface protein with a multi-domain extracellular region that mediates cell–cell and cell–matrix interactions. It is characterized by thrombospondin type-1 repeats (TSRs), a GAIN domain that promotes autoproteolytic cleavage, and a 7-transmembrane domain for signal transduction. ADGRB1/BAI1 inhibits angiogenesis (formation of blood vessels), especially in the brain, through its TSR domains, interacts with neuronal proteins to regulate synapse formation and maturation, and orchestrates signaling cascades for immune responses and cell adhesion. Alternative splicing yields several isoforms (full-length and truncated), which can have tissue-specific functions or disease relevance. The receptor represents an emerging therapeutic target for modulating angiogenesis and neurodevelopmental pathways, with further research ongoing to develop selective modulators. Key structural and mechanistic insights: Full-length form (173.5 kDa) features extracellular RGD motif, five TSRs, hormone-binding region, GAIN domain, and a 7TM core. Undergoes autoproteolytic cleavage to yield functionally active fragments. Intracellular loops and C-terminal domains interact with various signaling molecules (RhoA, Rac1, IRSp53, ELMO/DOCK180). Predominant in brain and vascular endothelium; reduced expression is linked to tumor angiogenesis and poor prognosis in gliomas. No major nomenclature errors or disease associations are absent in current literature. Precise drugs or inhibitors remain experimental, but the molecule is widely considered a druggable therapeutic target in specific disease settings.

Other names

Brain-specific angiogenesis inhibitor 1BAI1Vasculostatin-40 (Vstat40)Vasculostatin-120 (Vstat120)GDAIFADGRB1

Activation or inhibition of G protein-coupled signaling pathways through extracellular matrix or cell surface interactions; Signal transduction via intracellular domains, engaging Rho/Rac signaling; Angiogenesis inhibition through binding of thrombospondin repeats to endothelial cell partners (CD36, etc.)