Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E

@article{Letourneur1995StericMO,
  title={Steric masking of a dilysine endoplasmic reticulum retention motif during assembly of the human high affinity receptor for immunoglobulin E},
  author={Franck Letourneur and Silke Hennecke and Corinne D{\'e}molli{\`e}re and Pierre Cosson},
  journal={The Journal of Cell Biology},
  year={1995},
  volume={129},
  pages={971 - 978}
}
Signals that can cause retention in the ER have been found in the cytoplasmic domain of individual subunits of multimeric receptors destined to the cell surface. To study how ER retention motifs are masked during assembly of oligomeric receptors, we analyzed the assembly and intracellular transport of the human high-affinity receptor for immunoglobulin E expressed in COS cells. The cytoplasmic domain of the alpha chain contains a dilysine ER retention signal, which becomes nonfunctional after… CONTINUE READING

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