Ontology highlight
ABSTRACT:
SUBMITTER: Vembar SS
PROVIDER: S-EPMC2903355 | biostudies-literature | 2010 Jul
REPOSITORIES: biostudies-literature
Vembar Shruthi S SS Jonikas Martin C MC Hendershot Linda M LM Weissman Jonathan S JS Brodsky Jeffrey L JL
The Journal of biological chemistry 20100429 29
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. ...[more]