BiP‐dependent export of cholera toxin from endoplasmic reticulum‐derived microsomes

FEBS Letters

Herzog, Volker¹  Winkeler, Alexandra¹  Gödderz, Daniela¹  Schmitz, Anton¹ 

[1] Institut für Zellbiologie, Rheinische Friedrich-Wilhelms Universität Bonn, Ulrich-Haberland-Str. 61a, 53121 Bonn, Germany

关键词: Chaperone;    Cholera toxin;    Endoplasmic reticulum;    Translocation;    BiP;    heavy chain binding protein;    BiPrec;    recombinant BiP;    CT;    cholera toxin;    CTA;    CT subunit A;    CTA1;    CT subunit A1;    ER;    endoplasmic reticulum;    PDI;    protein disulfide isomerase;   

DOI  :  10.1016/S0014-5793(03)01217-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown