BAG2 overexpression 293T lysate (whole cell)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The BAG2 protein also known as Bcl-2-associated athanogene 2 is a co-chaperone that modulates the activity of heat shock proteins especially Hsp70. It has a molecular mass of approximately 27 kDa. BAG2 regulates the degradation of misfolded proteins by binding to the ATPase domain of Hsp70. It is expressed widely in human tissues including the brain heart and skeletal muscle suggesting its broad physiological importance.

Biological function summary

The role of BAG2 involves maintaining protein homeostasis a critical aspect of cellular functions. It forms a complex with Hsp70 assisting in the proper folding of newly synthesized proteins and preventing their aggregation. BAG2 also impacts the ubiquitin-proteasome system by blocking the association of Hsp70 with CHIP an E3 ubiquitin ligase. This regulation prevents the proteolytic degradation of client proteins.

Pathways

BAG2 functions within the cellular stress response and protein folding pathways. It has a significant involvement in the Hsp70-mediated protein folding pathway where it influences the fate of various substrate proteins. The interaction of BAG2 with Hsp70 and the ubiquitin-proteasome pathway highlights its contribution to cellular homeostasis. Additionally BAG2's modulation of these pathways suggests a link with apoptosis regulation where it associates indirectly with Bcl-2 family members.

BAG2 has been linked to neurodegenerative diseases such as Alzheimer's disease. The dysregulation of BAG2 expression and function could lead to the accumulation of misfolded proteins exacerbating neurodegeneration. BAG2 also associates with various cancers where its expression may impact tumor survival and resistance to stress. Its interaction with Hsp70 and Bcl-2 proteins plays a role in these pathologies influencing disease progression and therapeutic outcomes.