Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond

2009 ◽  
Vol 485 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Xinmiao Fu ◽  
Bao Ting Zhu
2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Marcel Van Lith ◽  
Dave Bown ◽  
John Gatehouse ◽  
Adam M Benham

2002 ◽  
Vol 159 (2) ◽  
pp. 207-216 ◽  
Author(s):  
Billy Tsai ◽  
Tom A. Rapoport

The toxic effect of cholera toxin (CT) on target cells is caused by its A1 chain. This polypeptide is released from the holotoxin and unfolded in the lumen of the ER by the action of protein disulfide isomerase (PDI), before being retrotranslocated into the cytosol. The polypeptide is initially unfolded by binding to the reduced form of PDI. We show that upon oxidation of the COOH-terminal disulfide bond in PDI by the enzyme Ero1, the A1 chain is released. Both yeast Ero1 and the mammalian Ero1α isoform are active in this reaction. Ero1 has a preference for the PDI–toxin complex. We further show that the complex is transferred to a protein at the lumenal side of the ER membrane, where the unfolded toxin is released from PDI by the action of Ero1. Taken together, our results identify Ero1 as the enzyme mediating the release of unfolded CT from PDI and characterize an additional step in retrotranslocation of the toxin.


1996 ◽  
Vol 15 (1) ◽  
pp. 9-16 ◽  
Author(s):  
MARK G. DESILVA ◽  
JIA LU ◽  
GIULIA DONADEL ◽  
WILLIAM S. MODI ◽  
HONG XIE ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document