BAG5
Domain
The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain.
Function
Co-chaperone for HSP/HSP70 proteins. It functions as a nucleotide-exchange factor promoting the release of ADP from HSP70, thereby activating HSP70-mediated protein refolding (PubMed:20223214). Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding (By similarity). Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity).
Involvement in disease
Cardiomyopathy, dilated, 2F
CMD2F
A form of dilated cardiomyopathy, a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. CMD2F is an autosomal recessive, early-onset form.
None
The disease is caused by variants affecting the gene represented in this entry.
Tissue Specificity
Expressed in the heart.
Cellular localization
- In cardiomyocytes, localized at specialized membrane contact sites between T-tubules and the sarcoplasmic reticulum, known as junctional membrane complexes.
Alternative names
KIAA0873, BAG5, BAG family molecular chaperone regulator 5, BAG-5, Bcl-2-associated athanogene 5