Assembly of immunoglobulin light chains as a prerequisite for secretion: a model for oligomerization-dependent subunit folding
K Leitzgen, MR Knittler, IG Haas - Journal of Biological Chemistry, 1997 - ASBMB
Oligomeric proteins usually have to assemble into their final quartenary structure to be
secreted. However, most immunoglobulin (Ig) light (L) chains can be exported as free
chains, whereas only a few Ig L chains, here referred to as export-incompetent, have to
assemble with Ig heavy (H) chains into antibody molecules to be secreted. In the absence of
Ig H chain expression, these export-incompetent Ig L chains remain bound to BiP as partially
folded monomers with only one of the two internal disulfide bonds being formed. To …
secreted. However, most immunoglobulin (Ig) light (L) chains can be exported as free
chains, whereas only a few Ig L chains, here referred to as export-incompetent, have to
assemble with Ig heavy (H) chains into antibody molecules to be secreted. In the absence of
Ig H chain expression, these export-incompetent Ig L chains remain bound to BiP as partially
folded monomers with only one of the two internal disulfide bonds being formed. To …
