The C-terminal Extension of a Hybrid Immunoglobulin A/G Heavy Chain Is Responsible for Its Golgi-mediated Sorting to the Vacuole
AUTOR(ES)
Hadlington, Jane L.
FONTE
The American Society for Cell Biology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=194906Documentos Relacionados
- Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide.
- Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA
- A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole.
- A Small C-Terminal Sequence of Aurora B Is Responsible for Localization and Function
- Mannose Analog 1-Deoxymannojirimycin Inhibits the Golgi-Mediated Processing of Bean Storage Glycoproteins 12