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- W2128300600 abstract "Hsp70 chaperones can potentially interact with one of several J domain-containing Hsp40 co-chaperones to regulate distinct cellular processes. However, features within Hsp70s that determine Hsp40 specificity are undefined. To investigate this question, we introduced mutations into the ER-lumenal Hsp70, BiP/Kar2p, and found that an R217A substitution in the J domain-interacting surface of BiP compromised the physical and functional interaction with Sec63p, an Hsp40 required for ER translocation. In contrast, interaction with Jem1p, an Hsp40 required for ER-associated degradation, was unaffected. Moreover, yeast expressing R217A BiP exhibited defects in translocation but not in ER-associated degradation. Finally, the genetic interactions of the R217A BiP mutant were found to correlate with those of known translocation mutants. Together, our results indicate that residues within the Hsp70 J domain-interacting surface help confer Hsp40 specificity, in turn influencing distinct chaperone-mediated cellular activities." @default.
- W2128300600 created "2016-06-24" @default.
- W2128300600 creator A5004896108 @default.
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- W2128300600 date "2010-07-01" @default.
- W2128300600 modified "2023-09-30" @default.
- W2128300600 title "J Domain Co-chaperone Specificity Defines the Role of BiP during Protein Translocation" @default.
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- W2128300600 doi "https://doi.org/10.1074/jbc.m110.102186" @default.
- W2128300600 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2903355" @default.
- W2128300600 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20430885" @default.
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