N-glycosylation and conserved cysteine residues in RAMP3 play a critical role for the functional expression of CRLR/RAMP3 adrenomedullin receptor

Results indicate that the receptor activity modifying protein-3 (RAMP-3) is assembled with the calcitoni receptor-like receptor (CRLR) to yield a multiple N-glycosylated species using 2 to 4 consensus sites. Data show that inefficient use of Asn28 and Asn57 consensus sites result in the expression of multiple N-glycosylated RAMP3 species and that N-glycans participate in CRLR/RAMP3 receptor's function.