Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval.

@article{Shenkman1997EndoplasmicRQ,
  title={Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval.},
  author={Marina Shenkman and Moshe Ayalon and Gerardo Z. Lederkremer},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 21},
  pages={11363-8}
}
The human asialoglycoprotein receptor H2a subunit contains a charged pentapeptide, EGHRG, in its ectodomain that is the only sequence absent from the H2b alternatively spliced variant. H2b exits the endoplasmic reticulum (ER) even when singly expressed, whereas H2a gives rise to a cleaved soluble secreted ectodomain fragment; uncleaved membrane-bound H2a molecules are completely retained and degraded in the ER. We have inserted the H2a pentapeptide into the sequence of the H1 subunit (H1i5… CONTINUE READING
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