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An interaction map of endoplasmic reticulum chaperones and foldases.


ABSTRACT: 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.

SUBMITTER: Jansen G 

PROVIDER: S-EPMC3434782 | biostudies-other | 2012 Sep

REPOSITORIES: biostudies-other

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An interaction map of endoplasmic reticulum chaperones and foldases.

Jansen Gregor G   Määttänen Pekka P   Denisov Alexey Y AY   Scarffe Leslie L   Schade Babette B   Balghi Haouaria H   Dejgaard Kurt K   Chen Leanna Y LY   Muller William J WJ   Gehring Kalle K   Thomas David Y DY  

Molecular & cellular proteomics : MCP 20120604 9


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. W  ...[more]

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