Inhibition of immunoglobin folding and secretion by dominant negative BiP ATPase mutants

Hendershot et al examine how the BiP protein interacts with immunoglobin light chain during its folding. The results indicate that light chains undergo both BiP-dependent and BiP-independent folding steps, demonstrating that both ATP binding and hydrolysis activities of BiP are essential for the completion of light chain folding in vivo.