Journal
FEBS LETTERS
Volume 554, Issue 3, Pages 439-442Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)01217-1
Keywords
chaperone; cholera toxin; endoplasmic reticulum; translocation
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Cholera toxin (CT) is transported from the cell surface to the endoplasmic reticulum (ER) from where it is translocated to the cytosol in a process depending on ATP and luminal ER proteins. To test whether the molecular chaperone BiP (heavy chain binding protein), which is an ER-luminal ATPase, was one of the required proteins the export of CT was analyzed using ER-derived CT-loaded microsomes. The resubstitution of extracted export-incompetent microsomes with purified BiP was sufficient to restore the export of CT. As BiP protected CT from aggregation it is proposed that BiP maintains CT in a soluble, export-competent state. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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