HspBP1 overexpression 293T lysate (whole cell)

Supplementary information

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

HspBP1 also known as Heat Shock Protein Binding Protein 1 acts mechanically as a co-chaperone that regulates the activity of Hsp70. It has a molecular mass of approximately 28 kDa. HspBP1 expression occurs in various tissues with significant levels found in tissues undergoing high cellular stress such as the brain and heart. It plays a role in modulating the chaperone activity of Hsp70 by promoting the release of ADP from the nucleotide-binding domain.

Biological function summary

HspBP1 influences protein folding and repair mechanisms in cells. It functions as part of a complex with Hsp70 facilitating the reduction of misfolded and damaged proteins within the cell. Through this interaction HspBP1 assists in maintaining cellular protein homeostasis especially under stressful conditions that might otherwise lead to protein misfolding and aggregation.

Pathways

HspBP1 joins the protein quality control and cellular stress response pathways. Its involvement with Hsp70 is important in these processes ensuring proper protein folding and preventing aggregation. This relationship becomes evident in pathways like the unfolded protein response and heat shock response with HspBP1 modulating activities alongside other chaperones and co-chaperones within these networks.

High or dysfunctional HspBP1 levels associate with neurodegenerative diseases and cancer. In neurodegenerative diseases altered HspBP1 can contribute to the accumulation of misfolded proteins exacerbating conditions such as Alzheimer's disease. Its interaction with Hsp70 is particularly critical in tumorigenesis where enhanced expression can affect tumor progression and therapy resistance.