Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.

@article{Nakamura1999RegulationOF,
  title={Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.},
  author={Fujio Nakamura and Laizhen Huang and K Pestonjamasp and Elisabeth J Luna and Heinz Furthmayr},
  journal={Molecular biology of the cell},
  year={1999},
  volume={10 8},
  pages={
          2669-85
        }
}
Activation of human platelets with thrombin transiently increases phosphorylation at (558)threonine of moesin as determined with phosphorylation state-specific antibodies. This specific modification is completely inhibited by the kinase inhibitor staurosporine and maximally promoted by the phosphatase inhibitor calyculin A, making it possible to purify the two forms of moesin to homogeneity. Blot overlay assays with F-actin probes labeled with either [32P]ATP or 125I show that only… CONTINUE READING
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In: Handbook of Surfactants, ed

  • T. Igarashi
  • T. Yoshida, S. Shindo, T. Ohgaki and T. Yamanaka…
  • 1987
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