Cytoplasmic domain of E-selectin contains a non-tyrosine endocytosis signal.

@article{Chuang1997CytoplasmicDO,
  title={Cytoplasmic domain of E-selectin contains a non-tyrosine endocytosis signal.},
  author={Peter I Chuang and Bradford A. Young and Ravi R Thiagarajan and Carla A Cornejo and Robert K. Winn and John Harlan},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 40},
  pages={24813-8}
}
E-selectin is an activation-dependent, endothelial cell-restricted adhesion molecule that is internalized and degraded rapidly once expressed on the cell surface. Tyrosine-containing structural motifs play an important role in the internalization of a number of integral proteins, and the membrane-proximal E-selectin cytoplasmic tyrosine residue (Tyr582) conforms to the endocytosis motif proposed previously. To determine the endocytosis motif in E-selectin, we selectively introduced truncation… CONTINUE READING

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