IDENTIFICATION OF N-GLYCOSYLATION SITES IN THE GONADOTROPIN-RELEASING-HORMONE RECEPTOR - ROLE IN RECEPTOR EXPRESSION BUT NOT LIGAND-BINDING

Citation
Js. Davidson et al., IDENTIFICATION OF N-GLYCOSYLATION SITES IN THE GONADOTROPIN-RELEASING-HORMONE RECEPTOR - ROLE IN RECEPTOR EXPRESSION BUT NOT LIGAND-BINDING, Molecular and cellular endocrinology, 107(2), 1995, pp. 241-245
Citations number
27
Categorie Soggetti
Endocrynology & Metabolism","Cell Biology
ISSN journal
03037207
Volume
107
Issue
2
Year of publication
1995
Pages
241 - 245
Database
ISI
SICI code
0303-7207(1995)107:2<241:IONSIT>2.0.ZU;2-Q
Abstract
The asparagine residues of the three N-glycosylation consensus sequenc es in the mouse gonadotropin-releasing hormone receptor were mutated t o determine which residues were glycosylated and the function of glyco sylation. Photoaffinity labelled Gln(4) and Gln(18) receptor mutants e xhibited lower apparent molecular weight on SDS polyacrylamide gel ele ctrophoresis, while the Gln(102) receptor showed wildtype mobility. Th is indicates that the receptor is glycosylated at Asn(4) and Asn(18) b ut not at Asn(102). Binding affinities of all the mutant receptors wer e normal, indicating that carbohydrate moieties are not involved in li gand binding interactions. However, expression of the Gln(4) and Gln(1 8) receptors were substantially decreased, indicating a role for glyco sylation in receptor expression or stability. All the glycosylation si te mutants were capable of normal signal transduction, as indicated by their ability to stimulate inositol phosphate production.