Hsp90perheet

Hsp90perheet refers to a family of heat shock proteins, specifically the Hsp90 proteins, and their associated chaperone machinery. Hsp90 proteins are highly conserved molecular chaperones found in all kingdoms of life. Their primary function is to assist in the proper folding, activation, and stabilization of a wide range of client proteins, many of which are involved in crucial cellular processes such as signal transduction, cell cycle control, and transcription.

The Hsp90 chaperone cycle involves a series of conformational changes driven by ATP hydrolysis and the action of co-chaperones. These co-chaperones, which are integral to the Hsp90perheet system, modulate Hsp90's ATPase activity and its interaction with client proteins. Examples of such co-chaperones include Hsp70, Hsp40, Hop, and p23.

Hsp90 proteins are essential for cell viability and are often upregulated under conditions of cellular stress, such as heat shock, hence their name. However, their role extends beyond stress response. They are critical for maintaining the integrity and function of many oncogenic proteins, making them attractive targets for cancer therapy. Inhibiting Hsp90 function can lead to the degradation of these client proteins, thereby disrupting cancer cell growth and survival. The study of Hsp90perheet is therefore of significant interest in both fundamental cell biology and therapeutic development.