Interaction between platelet glycoprotein Ibalpha and filamin-1 is essential for glycoprotein Ib/IX receptor anchorage at high shear.

@article{Williamson2002InteractionBP,
  title={Interaction between platelet glycoprotein Ibalpha and filamin-1 is essential for glycoprotein Ib/IX receptor anchorage at high shear.},
  author={David Williamson and Inna Pikovski and Susan L. Cranmer and Pierre Mangin and Nayna Mistry and Teresa Domagala and Sam Chehab and François Lanza and Hatem H. Salem and Shaun P Jackson},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 3},
  pages={
          2151-9
        }
}
The interaction of the glycoprotein (GP) Ib-V-IX receptor complex with the membrane skeleton of platelets is dependent on a specific interaction between the cytoplasmic tail of GPIbalpha and filamin-1. This interaction has been proposed to regulate key aspects of platelet function, including the ligand binding of GPIb-V-IX and the ability of the cells to sustain adhesion to von Willebrand factor (vWf) under high shear. In this study we have examined sequences in the GPIbalpha intracellular… CONTINUE READING
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