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N‐linked glycosylation of platelet P 2 Y 12 ADP receptor is essential for signal transduction but not for ligand binding or cell surface expression
Author(s) -
Zhong Xiaotian,
Kriz Ron,
Seehra Jasbir,
Kumar Ravindra
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00191-7
Subject(s) - tunicamycin , adenylyl cyclase , receptor , signal transduction , n linked glycosylation , glycosylation , chemistry , biochemistry , 5 ht5a receptor , ligand (biochemistry) , biology , microbiology and biotechnology , glycan , glycoprotein , gene , unfolded protein response
P 2 Y 12 receptor is a G i ‐coupled adenosine diphosphate (ADP) receptor with a critical role in platelet aggregation. It contains two potential N‐linked glycosylation sites at its extra cellular amino‐terminus, which may modulate its activity. Studies of both tunicamycin treatment and site‐directed mutagenesis have revealed a dispensable role of the N‐linked glycosylation in the receptor's surface expression and ligand binding activity. However, the non‐glycosylated P 2 Y 12 receptor is defective in the P 2 Y 12 ‐mediated inhibition of the adenylyl cyclase activity. Thus the study uncovers an unexpected vital role of N‐linked glycans in receptor's signal transducing step but not in surface expression or ligand binding.