Stress-Induced-Phosphoprotein 1 Protein

Background

STIP1 is a co-chaperone protein that coordinates the activities of heat shock proteins HSP70 and HSP90, facilitating protein folding, stability, and transport under stress conditions. It functions as a scaffold protein that regulates the transfer of client proteins between HSP70 and HSP90, ensuring proper protein maturation, stabilization, and degradation. STIP1 is ubiquitously expressed and is critical for processes such as protein quality control, cellular stress responses, and signal transduction. It also plays a role in cancer progression, where it stabilizes oncogenic signaling proteins and promotes tumor cell survival and proliferation. Dysregulation of STIP1 is associated with neurodegenerative diseases, such as Huntington's and Alzheimer's, where impaired chaperone function leads to protein aggregation and cellular dysfunction. Knockout studies reveal increased sensitivity to stress, defects in protein homeostasis, and impaired cell viability, emphasizing its role in protein folding, stress response, and maintaining cellular proteostasis.