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Published 19 June 2006. doi:10.1083/jcb.200602046
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 6, 853-859
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 Protein disulfide isomerase–like proteins play opposing roles during retrotranslocation

Michele L. Forster1, Kelsey Sivick2, Young-nam Park3, Peter Arvan3, Wayne I. Lencer4, and Billy Tsai1

1 Department of Cell and Developmental Biology, 2 Department of Microbiology and Immunology, and 3 Division of Metabolism, Endocrinology, and Diabetes, University of Michigan Medical School, Ann Arbor, MI 48109
4 GI Cell Biology, Children's Hospital, Harvard Medical School, Boston, MA 02115

Correspondence to Billy Tsai: btsai{at}umich.edu

Misfolded proteins in the endoplasmic reticulum (ER) are retained in the organelle or retrotranslocated to the cytosol for proteasomal degradation. ER chaperones that guide these opposing processes are largely unknown. We developed a semipermeabilized cell system to study the retrotranslocation of cholera toxin (CT), a toxic agent that crosses the ER membrane to reach the cytosol during intoxication. We found that protein disulfide isomerase (PDI) facilitates CT retrotranslocation, whereas ERp72, a PDI-like protein, mediates its ER retention. In vitro analysis revealed that PDI and ERp72 alter CT's conformation in a manner consistent with their roles in retrotranslocation and ER retention. Moreover, we found that PDI's and ERp72's opposing functions operate on endogenous ER misfolded proteins. Thus, our data identify PDI family proteins that play opposing roles in ER quality control and establish an assay to further delineate the mechanism of CT retrotranslocation.

Abbreviations used in this paper: BFA, brefeldin A; CT, cholera toxin; NEM, N-ethylmaleimide; PDI, protein disulfide isomerase; Tg, thyroglobulin.


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