First published online October 30, 2006
Journal of Cell Science 119, 2105e (2006)
© The Company of Biologists Limited
DABbling with integrin function
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
and
granules. Interactions between fibrinogen and integrin
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
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
granules. During platelet activation, they report, DAB2 is released and binds to the extracellular region of
IIbß3 integrin. Because this binding involves the part of
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
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]