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Article

J domain co-chaperone specificity defines the role of BiP during protein translocation.

The Journal of biological chemistry - 16 Jul 2010

Vembar Shruthi S, Jonikas Martin C, Hendershot Linda M, Weissman Jonathan S, Brodsky Jeffrey L

Abstract excerpt

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...

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Identifiers

PMID: 20430885
DOI: 10.1074/jbc.M110.102186
PMCID: PMC2903355

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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J domain co-chaperone specificity defines the role of BiP during protein translocation.PMID 20430885Read ↗

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