NS 1619, KCa1.1 channel activator

Supplementary information

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

Hsp90 also known as Heat Shock Protein 90 is a molecular chaperone with a mass of approximately 90 kDa. It plays a role in stabilizing and activating client proteins which are often involved in signal transduction. Hsp90 is found in the cytoplasm of eukaryotic cells and is highly expressed in response to stress. It is essential for maintaining cellular protein homeostasis under normal and stress conditions.

Biological function summary

Hsp90 interacts with various client proteins to facilitate their correct folding maturation activation and stabilization. It is a part of a chaperone complex that includes co-chaperones such as Cdc37 and p23 which aid in its function. Hsp90 influences several cellular processes including cell cycle control and apoptosis. Its involvement in these processes makes it a critical player in cellular regulation and adaptation.

Pathways

Hsp90 is integral to the MAPK and PI3K/AKT signaling pathways. It interacts with related proteins like Raf-1 and Akt ensuring their proper folding and function. Through these pathways Hsp90 supports cellular growth and survival playing a significant role in signal transduction and cellular response to external stimuli.

Hsp90 is often implicated in cancer and neurodegenerative diseases. Its overexpression is linked to cancer progression as it stabilizes several oncogenic client proteins like HER2. In neurodegenerative diseases Hsp90 interacts with proteins such as Tau and huntingtin; improper regulation can lead to disease progression. These associations highlight Hsp90's potential as a therapeutic target for various pathological conditions.