BAG5
Description
The BAG5 (BAG cochaperone 5) is a protein-coding gene located on chromosome 14.
BAG5 (BAG family molecular chaperone regulator 5) is a protein encoded by the BAG5 gene in humans. It belongs to the BAG1-related protein family, which includes anti-apoptotic proteins like BAG1. BAG1 interacts with various cellular proteins involved in apoptosis and growth, such as BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors, and members of the heat shock protein 70 kDa family. BAG5 contains a BAG domain near its C-terminus, which can bind and inhibit the chaperone activity of Hsc70/Hsp70. There are three transcript variants of the BAG5 gene, resulting in two different isoforms.
BAG5 functions as a co-chaperone for HSP/HSP70 proteins, promoting the release of ADP from HSP70 and activating HSP70-mediated protein refolding. It plays a crucial role in maintaining proteostasis at junctional membrane complexes (JMCs), acting as a scaffold between the HSPA8 chaperone and JMC proteins to ensure correct protein folding. Additionally, BAG5 inhibits both the auto-ubiquitination of PRKN and the ubiquitination of target proteins by PRKN.
BAG5 is also known as BAG-5, CMD2F.
