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First published online October 30, 2006


Journal of Cell Science 119, 2105e (2006)
© The Company of Biologists Limited
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DABbling with integrin function


Figure 1

Platelet aggregation plays an important role in blood clotting. When a blood vessel is damaged, platelets are recruited to the injured endothelium, where they release coagulation factors and platelet activation factors from their {alpha} and {delta} granules. Interactions between fibrinogen and integrin {alpha}IIbß3 on the surface of platelets then induce platelet aggregation, which helps to form a clot. On p. 4420, Ching-Ping Tseng and colleagues reveal that the adaptor protein, Disabled-2 (DAB2) negatively regulates these interactions by binding to {alpha}IIb integrin on the platelet surface. DAB2 is best known as a cytoplasmic adaptor. The authors now show that it is also present in platelet {alpha} granules. During platelet activation, they report, DAB2 is released and binds to the extracellular region of {alpha}IIbß3 integrin. Because this binding involves the part of {alpha}IIb integrin that binds to fibrinogen, DAB2 blocks the platelet-fibrinogen interaction and thus inhibits platelet aggregation. The authors propose therefore that DAB2 helps to regulate the size of platelet aggregates, which could prevent excessive clotting.


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Related articles in JCS:

Disabled-2 is a novel {alpha}IIb-integrin-binding protein that negatively regulates platelet-fibrinogen interactions and platelet aggregation
Chien-Ling Huang, Ju-Chien Cheng, Arnold Stern, Jer-Tsong Hsieh, Chang-Hui Liao, and Ching-Ping Tseng
JCS 2006 119: 4420-4430. [Abstract] [Full Text]  




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