Large proline-rich protein BAG6

BAG6 (Large proline-rich protein BAG6) is an ATP-independent molecular chaperone that prevents aggregation of misfolded proteins and mediates their proper delivery to the endoplasmic reticulum or proteasome (UniProt: P46379). It functions as part of the BAG6/BAT3 quality control complex, which is critical for handling tail-anchored proteins, endoplasmic reticulum-associated degradation, and ER stress responses. BAG6 also participates in DNA damage-induced apoptosis and immune regulation via natural killer cell activation.

BAG6 operates across multiple cellular compartments and pathways, including protein quality control, ER homeostasis, and apoptotic signaling (UniProt: P46379). The protein has no curated disease associations in UniProt's structured disease field.

In Alzheimer's Disease, BAG6 is significantly downregulated in post-mortem AD brain tissue compared to age-matched controls (Chaparral AD proteomics), with a mean log2 fold-change of −0.35. This reduced expression may compromise protein quality control mechanisms in AD, potentially contributing to the accumulation of misfolded proteins characteristic of the disease.