Tyrphostin A23 inhibits internalization of the transferrin receptor by perturbing the interaction between tyrosine motifs and the medium chain subunit of the AP-2 adaptor complex.

@article{Banbury2003TyrphostinAI,
  title={Tyrphostin A23 inhibits internalization of the transferrin receptor by perturbing the interaction between tyrosine motifs and the medium chain subunit of the AP-2 adaptor complex.},
  author={David N Banbury and Jacqueline D Oakley and Richard B. Sessions and George Banting},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 14},
  pages={12022-8}
}
Several intracellular membrane trafficking events are mediated by tyrosine-containing motifs within the cytosolic domains of integral membrane proteins. Many such motifs conform to the consensus YXXPhi, where Phi represents a bulky hydrophobic residue. This motif interacts with the medium chain (mu) subunits of adaptor complexes that link the cytosolic domains of integral membrane proteins to the clathrin coat involved in vesicle formation. The YXXPhi motif is similar to motifs in which the… CONTINUE READING
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