Modulation of FcgammaRI (CD64) ligand binding by blocking peptides of periplakin.

  title={Modulation of FcgammaRI (CD64) ligand binding by blocking peptides of periplakin.},
  author={Jeffrey Matthijn Beekman and Jantine E. Bakema and Joke A van der Linden and Bastiaan B. J. Tops and Marja Hinten and Martine J van Vugt and Jan G. J. van de Winkel and Jeanette H W Leusen},
  journal={The Journal of biological chemistry},
  volume={279 32},
FcgammaRI requires both the intracellular domain of the alpha-chain and associated leukocyte Fc receptor (FcR) gamma-chains for its biological function. We recently found the C terminus of periplakin to selectively interact with the cytoplasmic domain of the FcgammaRI alpha-chain. It thereby enhances the capacity of FcgammaRI to bind, internalize, and present antigens on MHC class II. Here, we characterized the domains involved in FcgammaRI-periplakin interaction using truncated and alanine… CONTINUE READING

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