RGD Reference Report - An interaction map of endoplasmic reticulum chaperones and foldases. - Rat Genome Database

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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.
RGD ID: 8553430
Pubmed: PMID:22665516   (View Abstract at PubMed)
PMCID: PMC3434782   (View Article at PubMed Central)
DOI: DOI:10.1074/mcp.M111.016550   (Journal Full-text)

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.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Pdia4Ratchaperone-mediated protein folding involved_inIDA PMID:22665516UniProt 

Cellular Component

  

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Calr  (calreticulin)
Canx  (calnexin)
Dnajc3  (DnaJ heat shock protein family (Hsp40) member C3)
Erp29  (endoplasmic reticulum protein 29)
Hsp90b1  (heat shock protein 90 beta family member 1)
Hspa5  (heat shock protein family A (Hsp70) member 5)
Hyou1  (hypoxia up-regulated 1)
Pdia3  (protein disulfide isomerase family A, member 3)
Pdia4  (protein disulfide isomerase family A, member 4)
Pdia6  (protein disulfide isomerase family A, member 6)
Ppib  (peptidylprolyl isomerase B)
Prdx4  (peroxiredoxin 4)


Additional Information