J-proteins are a class of molecular chaperones that serve to stimulate the activity of Hsp70s and are often located to recruit Hsp70 to a particular cellular function. Protein degradation associated with the endoplasmic reticulum (ERAD) is one such cellular process that requires Hsp70 on both faces of the endoplasmic reticulum. At least five J-proteins, including Jid1 (DnaJ protein Involved in ER-associated Degradation), have been implicated in controlling ERAD. Here we show that Jid1 is confined within the mitochondrial matrix - Jid1 has the same topology as the J-proteins Pam18 and Mdj2, which stimulate mitochondrial Hsp70 to drive protein import into the mitochondrial matrix. The location of Jid1 within mitochondria makes it unavailable to participate directly in the regulation of ERAD.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|