Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zhong X,Kriz R,Seehra J,Kumar Rdoi
10.1016/S0014-5793(04)00191-7keywords:
subject
Has Abstractpub_date
2004-03-26 00:00:00pages
111-7issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579304001917journal_volume
562pub_type
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