Renhao Li Lab:Research: Difference between revisions
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==Structure and Regulation of Platelet GPIb-IX-V Complex== | |||
The glycoprotein (GP)Ib-IX-V complex (a.k.a. CD42) is one of the major hubs on the platelet surface for its aggregation and activation. Malfunction or lack of the GPIb-IX-V complex in platelets results in severe bleeding disorders, and it plays a critical role in a number of cardiovascular diseases including myocardial infarction and stroke. The interaction between the glycoprotein (GP)Ib-IX-V complex on the platelet surface and von Willebrand factor (VWF) that marks the injury site in the artery is widely considered as the first step for hemostasis. Upon binding to VWF, the GPIb-IX-V complex transduces into the platelet an activating signal, leading eventually to platelet aggregation and thrombus formation. The GPIb-IX-V complex consists of nine subunits of four kinds: GPIbα, GPIbβ, GPIX and GPV. Our current focus is to delineate the 3-dimensional organization of the complex, that is, how these subunits evolve, interact with one another and assemble into the functional receptor complex. The insights on the overall organization of the GPIb-IX-V complex will help us understand how it mediates signals of VWF-binding across the plasma membrane to activate the platelet, and how the binding activity of this complex is regulated by intracellular signals. | |||
We recently | |||
Revision as of 09:55, 16 September 2011
Structure and Regulation of Platelet GPIb-IX-V Complex
The glycoprotein (GP)Ib-IX-V complex (a.k.a. CD42) is one of the major hubs on the platelet surface for its aggregation and activation. Malfunction or lack of the GPIb-IX-V complex in platelets results in severe bleeding disorders, and it plays a critical role in a number of cardiovascular diseases including myocardial infarction and stroke. The interaction between the glycoprotein (GP)Ib-IX-V complex on the platelet surface and von Willebrand factor (VWF) that marks the injury site in the artery is widely considered as the first step for hemostasis. Upon binding to VWF, the GPIb-IX-V complex transduces into the platelet an activating signal, leading eventually to platelet aggregation and thrombus formation. The GPIb-IX-V complex consists of nine subunits of four kinds: GPIbα, GPIbβ, GPIX and GPV. Our current focus is to delineate the 3-dimensional organization of the complex, that is, how these subunits evolve, interact with one another and assemble into the functional receptor complex. The insights on the overall organization of the GPIb-IX-V complex will help us understand how it mediates signals of VWF-binding across the plasma membrane to activate the platelet, and how the binding activity of this complex is regulated by intracellular signals.
We recently
