Abstract：
:Cholera toxin is assembled from two subunits in the periplasm of Vibrio cholerae and disassembled in the analogous compartment of target cells, the lumen of the endoplasmic reticulum (ER), before a fragment of it, the A1 chain, is transported into the cytosol. We show that protein disulfide isomerase (PDI) in the ER lumen functions to disassemble and unfold the toxin once its A chain has been cleaved. PDI acts as a redox-driven chaperone; in the reduced state, it binds to the A chain and in the oxidized state it releases it. Our results explain the pathway of cholera toxin, suggest a role for PDI in retrograde protein transport into the cytosol, and indicate that PDI can act as a novel type of chaperone, whose binding and release of substrates is regulated by a redox, rather than an ATPase, cycle.
journal_name
Celljournal_title
Cellauthors
Tsai B,Rodighiero C,Lencer WI,Rapoport TAdoi
10.1016/s0092-8674(01)00289-6subject
Has Abstractpub_date
2001-03-23 00:00:00pages
937-48issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(01)00289-6journal_volume
104pub_type
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