Breaking the integrin hinge. A defined structural constraint regulates integrin signaling.

@article{Hughes1996BreakingTI,
  title={Breaking the integrin hinge. A defined structural constraint regulates integrin signaling.},
  author={Paul E. Hughes and Federico D{\'i}az-Gonz{\'a}lez and Lilley N Leong and Chuanyue Wu and John Alan McDonald and Sanford J Shattil and Mark H Ginsberg},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 12},
  pages={6571-4}
}
Integrins are heterodimeric (alpha, beta) cell adhesion receptors. We demonstrate that point mutations in the cytoplasmic domains of both the alpha and beta subunits promote constitutive signaling by the integrin alphaIIbbeta3. By generating charge reversal mutations, we show these "activating" mutations may act by disrupting a potential salt bridge between the membrane-proximal portions of the alpha and beta subunit cytoplasmic domains. Thus, the modulation of specific interactions between the… CONTINUE READING
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