The C-terminal extension of a hybrid immunoglobulin A/G heavy chain is responsible for its golgi-mediated sorting to the vacuole
UNSPECIFIED. (2003) The C-terminal extension of a hybrid immunoglobulin A/G heavy chain is responsible for its golgi-mediated sorting to the vacuole. MOLECULAR BIOLOGY OF THE CELL, 14 (6). pp. 2592-2602. ISSN 1059-1524Full text not available from this repository.
Official URL: http://dx.doi.org/10.1091/mbc.E02-11-0771
We have assessed the ability of the plant secretory pathway to handle the expression of complex heterologous proteins by investigating the fate of a hybrid immunoglobulin A/G in tobacco cells, Although plant cells can express large amounts of the antibody, a relevant proportion is normally lost to vacuolar sorting and degradation, Here we show that the synthesis of high amounts of IgA/G does not impose stress on the plant secretory pathway. Plant cells can assemble antibody chains with high efficiency and vacuolar transport occurs only after the assembled immunoglobulins have traveled through the Golgi complex. We prove that vacuolar delivery of IgA/G depends on the presence of a cryptic sorting, signal in the tailpiece of the IgA/G heavy chain. We also show that unassembled light chains are efficiently secreted as monomers by the plant secretory pathway.
|Item Type:||Journal Article|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Journal or Publication Title:||MOLECULAR BIOLOGY OF THE CELL|
|Publisher:||AMER SOC CELL BIOLOGY|
|Official Date:||June 2003|
|Number of Pages:||11|
|Page Range:||pp. 2592-2602|
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