Calmodulin interacts with the platelet ADP receptor P2Y1 |
| |
Authors: | Arthur Jane F Shen Yang Mu Fi-Tjen Leon Catherine Gachet Christian Berndt Michael C Andrews Robert K |
| |
Affiliation: | Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia. jane.arthur@med.monash.edu.au |
| |
Abstract: | P2Y1 [P2 (purinergic type-2)-receptor 1] is a G-protein-coupled ADP receptor that regulates platelet activation and ADP-induced Ca2+ signalling. Studies using P2Y1-knockout mice, G(q)-deficient mice or P2Y1-selective inhibitors have previously identified a key role for P2Y1 in pathophysiological thrombus formation at high shear stress. We provide evidence that a positively charged juxtamembrane sequence within the cytoplasmic C-terminal tail of P2Y1 can bind directly to the cytosolic regulatory protein calmodulin. Deletion by mutagenesis of the calmodulin-binding domain of P2Y1 inhibits intracellular Ca2+ flux in transfected cells. These results suggest that the interaction of calmodulin with the P2Y1 C-terminal tail may regulate P2Y1-dependent platelet aggregation. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|