Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations.

  title={Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations.},
  author={Renhao Li and Neal Mitra and Holly Gratkowski and Gaston Vilaire and Rustem I. Litvinov and Chandrasekaran Nagasami and John W. Weisel and James D. Lear and William F. DeGrado and Joel S. Bennett},
  volume={300 5620},
Transmembrane helices of integrin alpha and beta subunits have been implicated in the regulation of integrin activity. Two mutations, glycine-708 to asparagine-708 (G708N)and methionine-701 to asparagine-701, in the transmembrane helix of the beta3 subunit enabled integrin alphaIIbbeta3 to constitutively bind soluble fibrinogen. Further characterization of the G708N mutant revealed that it induced alphaIIbbeta3 clustering and constitutive phosphorylation of focal adhesion kinase. This mutation… CONTINUE READING

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