[HTML][HTML] Glycosylation of human truncated Fc∊ RI α chain is necessary for efficient folding in the endoplasmic reticulum (∗)
O Letourneur, S Sechi, J Willette-Brown… - Journal of Biological …, 1995 - ASBMB
The high affinity immunoglobulin E (IgE) receptor is an αβγ 2 tetrameric complex. The
truncated extracellular segment (αt) of the heavily glycosylated α chain is sufficient for high
affinity binding of IgE. Here we have expressed various αt mutants in eukaryotic and
prokaryotic cells to analyze the role of glycosylation in the folding, stability, and secretion of
αt. All seven N-linked glycosylation sites in αt are glycosylated and their mutations have an
additive effect on the folding and secretion of αt. Mutation of the seven N-glycosylation sites …
truncated extracellular segment (αt) of the heavily glycosylated α chain is sufficient for high
affinity binding of IgE. Here we have expressed various αt mutants in eukaryotic and
prokaryotic cells to analyze the role of glycosylation in the folding, stability, and secretion of
αt. All seven N-linked glycosylation sites in αt are glycosylated and their mutations have an
additive effect on the folding and secretion of αt. Mutation of the seven N-glycosylation sites …