Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors.
(2002) The EMBO journal — Vol. 21, n° 4, p. 504-513 (2002)
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- Abstract
- 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.
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Costagliola, S., Panneels, V., Bonomi, M., Koch, J., Many, M.-C., Smits, G., & Vassart, G. (2002). Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors. The EMBO journal, 21(4), 504-513. https://doi.org/10.1093/emboj/21.4.504 (Original work published 2002)