Publications by authors named "Yue-Tong Xi"
Androgens, such as 5α-dihydrotestosterone (5α-DHT), regulate numerous functions by binding to nuclear androgen receptors (ARs) and potential unknown membrane receptors. Here, we report that the androgen 5α-DHT activates membrane receptor GPR133 in muscle cells, thereby increasing intracellular cyclic AMP (cAMP) levels and enhancing muscle strength. Further cryoelectron microscopy (cryo-EM) structural analysis of GPR133-Gs in complex with 5α-DHT or its derivative methenolone (MET) reveals the structural basis for androgen recognition.
View Article and Find Full Text PDFAdhesion G protein-coupled receptors are elusive in terms of their structural information and ligands. Here, we solved the cryogenic-electron microscopy (cryo-EM) structure of apo-ADGRG2, an essential membrane receptor for maintaining male fertility, in complex with a G trimer. Whereas the formations of two kinks were determinants of the active state, identification of a potential ligand-binding pocket in ADGRG2 facilitated the screening and identification of dehydroepiandrosterone (DHEA), dehydroepiandrosterone sulfate and deoxycorticosterone as potential ligands of ADGRG2.
View Article and Find Full Text PDFArticle Synopsis
- Adhesion G-protein-coupled receptors (aGPCRs) play vital roles in various biological processes, and their activation often involves a specific internal sequence called the Stachel sequence which assumes a unique structural formation in their binding sites.
- Researchers used cryogenic electron microscopy to study two aGPCRs, GPR133 and GPR114, revealing that the Stachel sequences interact with specific motifs in their transmembrane domains, critical for receptor activation.
- The study identifies key mechanisms in how these receptors are activated and couple with G proteins, particularly highlighting a common binding interface and unique structural features of GPR114 that facilitate its interactions.