par Costagliola, Sabine 
;Panneels, Valérie;Bonomi, M;Koch, J;Many, Marie-Christine;Smits, Guillaume ;Vassart, Gilbert
Référence EMBO journal, 21, 4, page (504-513)
Publication Publié, 2002-02
;Panneels, Valérie;Bonomi, M;Koch, J;Many, Marie-Christine;Smits, Guillaume ;Vassart, Gilbert Référence EMBO journal, 21, 4, page (504-513)
Publication Publié, 2002-02
Article révisé par les pairs
| Résumé : | The glycoprotein hormone receptors (thyrotrophin receptor, TSHr; luteinizing hormone/chorionic gonadotrophin receptor, LH/CGr; follicle-stimulating hormone receptor, FSHr) constitute a subfamily of rhodopsin-like G protein-coupled receptors (GPCRs) with a long N-terminal extracellular extension responsible for high-affinity hormone binding. These ectodomains contain two cysteine clusters flanking nine leucine-rich repeats (LRR), a motif found in several protein families involved in protein-protein interactions. Similar to the situation described recently in CCR5, we demonstrate here that the TSHr, as it is present at the cell surface, is sulfated on tyrosines in a motif located downstream of the C-terminal cysteine cluster. Sulfation of one of the two tyrosines in the motif is mandatory for high-affinity binding of TSH and activation of the receptor. Site-directed mutagenesis experiments indicate that the motif, which is conserved in all members of the glycoprotein hormone receptor family, seems to play a similar role in the LH/CG and FSH receptors. |
