Residues throughout the cytoplasmic domain affect the internalization efficiency of P-selectin.

@article{Setiadi1995ResiduesTT,
  title={Residues throughout the cytoplasmic domain affect the internalization efficiency of P-selectin.},
  author={Hendra Setiadi and M Disdier and Sarah A Green and William Canfield and Rodger P McEver},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 45},
  pages={26818-26}
}
The cytoplasmic domains of many membrane proteins have short sequences, usually including a tyrosine or a di-leucine, that function as sorting signals. P-selectin is an adhesion receptor for leukocytes that is expressed on activated platelets and endothelial cells. Its 35-residue cytoplasmic domain contains signals for sorting into regulated secretory granules, for endocytosis, and for movement from endosomes to lysosomes. The domain has a membrane-distal sequence, YGVFTNAAF, that resembles… CONTINUE READING

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