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.
Original language | English |
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Pages (from-to) | 504-513 |
Number of pages | 10 |
Journal | EMBO Journal |
Volume | 21 |
Issue number | 4 |
DOIs | |
Publication status | Published - Feb 15 2002 |
Keywords
- Glycoprotein
- GPCR
- Hormones
- Sulfation
- Tyrosine
ASJC Scopus subject areas
- Genetics
- Cell Biology