Journal
IMMUNITY
Volume 15, Issue 1, Pages 105-114Publisher
CELL PRESS
DOI: 10.1016/S1074-7613(01)00163-7
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Funding
- NCI NIH HHS [CA21765] Funding Source: Medline
- NIGMS NIH HHS [GM54068] Funding Source: Medline
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Unassembled Ig heavy chains are retained in the ER via the binding of BiP to the C(H)1 domain, which remains unoxidized. Interestingly, this domain folds rapidly, albeit nonproductively, when heavy chains are released from BiP in vitro with ATP. The in vivo cycling of BiP from heavy chains was monitored using BiP ATPase mutants as kinetic traps. Our data suggest that BiP does not cycle from the CH1 domain of free heavy chains. However, heavy and light chain assembly occurs rapidly and requires the ATP-dependent release of BiP. We propose that BiP's ATPase cycle is stalled or nonproductive when it is bound to free heavy chains. The binding of light chains to the complex reactivates the cycle and releases BiP.
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