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An interaction map of endoplasmic reticulum chaperones and foldases.

Authors: Jansen, G  Maattanen, P  Denisov, AY  Scarffe, L  Schade, B  Balghi, H  Dejgaard, K  Chen, LY  Muller, WJ  Gehring, K  Thomas, DY 
Citation: Jansen G, etal., Mol Cell Proteomics. 2012 Sep;11(9):710-23. doi: 10.1074/mcp.M111.016550. Epub 2012 Jun 4.
Pubmed: (View Article at PubMed) PMID:22665516
DOI: Full-text: DOI:10.1074/mcp.M111.016550

Chaperones and foldases in the endoplasmic reticulum (ER) ensure correct protein folding. Extensive protein-protein interaction maps have defined the organization and function of many cellular complexes, but ER complexes are under-represented. Consequently, chaperone and foldase networks in the ER are largely uncharacterized. Using complementary ER-specific methods, we have mapped interactions between ER-lumenal chaperones and foldases and describe their organization in multiprotein complexes. We identify new functional chaperone modules, including interactions between protein-disulfide isomerases and peptidyl-prolyl cis-trans-isomerases. We have examined in detail a novel ERp72-cyclophilin B complex that enhances the rate of folding of immunoglobulin G. Deletion analysis and NMR reveal a conserved surface of cyclophilin B that interacts with polyacidic stretches of ERp72 and GRp94. Mutagenesis within this highly charged surface region abrogates interactions with its chaperone partners and reveals a new mechanism of ER protein-protein interaction. This ability of cyclophilin B to interact with different partners using the same molecular surface suggests that ER-chaperone/foldase partnerships may switch depending on the needs of different substrates, illustrating the flexibility of multichaperone complexes of the ER folding machinery.

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CRRD Object Information
CRRD ID: 8553430
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.