Tyrosine sulfation is required for agonist recognition by glycoprotein hormone receptors

S. Costagliola, V. Panneels, M. Bonomi, J. Koch, M. C. Many, G. Smits, G. Vassart

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)504-513
Number of pages10
JournalEMBO Journal
Issue number4
Publication statusPublished - Feb 15 2002


  • Glycoprotein
  • GPCR
  • Hormones
  • Sulfation
  • Tyrosine

ASJC Scopus subject areas

  • Genetics
  • Cell Biology


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