Downstream signaling molecules bind to different phosphorylated immunoreceptor tyrosine-based activation motif (ITAM) peptides of the high affinity IgE receptor.

@article{Kimura1996DownstreamSM,
  title={Downstream signaling molecules bind to different phosphorylated immunoreceptor tyrosine-based activation motif (ITAM) peptides of the high affinity IgE receptor.},
  author={Toshihiro Kimura and Hayato Kihara and Sucharita Bhattacharyya and Hiroshi Sakamoto and Ettore Appella and Reuben P. Siraganian},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 44},
  pages={27962-8}
}
The cytoplasmic tails of both the beta and gamma subunits of the high affinity IgE receptor (FcepsilonRI) contain a consensus sequence termed the immunoreceptor tyrosine-based activation motif (ITAM). This motif plays a critical role in receptor-mediated signal transduction. Synthetic peptides based on the ITAM sequences of the beta and gamma subunits of FcepsilonRI were used to investigate which proteins associate with these motifs. Tyrosine-phosphorylated beta and gamma ITAM peptides… CONTINUE READING

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