Title : N-glycosylation and disulfide bonding affects
GPRC6A receptor expression, function, and dimerization
Abstract :
- Investigation of post-translational modifications of receptor proteins is important for our understanding of receptor pharmacology and disease physiology
- However, our knowledge about post-translational modifications of class C G protein-coupled receptors and how these modifications regulate expression and function is very limited
- Herein, we show that the nutrient-sensing class C G protein-coupled receptor GPRC6A carries seven N-glycans and that one of these sites modulates surface expression whereas mutation of another site affects receptor function
- GPRC6A has been speculated to form covalently linked dimers through cysteine disulfide linkage in the extracellular amino-terminal domain and here we show that GPRC6A indeed is a homodimer and that a disulfide bridge between the C131 residues is formed
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. N-glycosylation, , GPRC6A receptor, -, -
- 3. carries, , GPRC6A, seven N-glycans, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):