Mouse STIP1 Homology And U-Box Containing Protein 1 (STUB1) Protein

Background

STUB1, also known as CHIP (C-terminus of Hsc70-interacting protein), is a co-chaperone protein and E3 ubiquitin ligase that regulates protein homeostasis by linking the molecular chaperones HSP70 and HSP90 to the ubiquitin-proteasome system. STUB1 promotes the ubiquitination and degradation of misfolded, damaged, or surplus proteins, ensuring proper protein quality control and cellular stress responses. It is broadly expressed in tissues and plays a crucial role in proteostasis, particularly under stress conditions where protein misfolding is elevated. STUB1 is also involved in signaling pathways regulating apoptosis, cell survival, and metabolic adaptation by targeting key signaling proteins for degradation. Dysregulation of STUB1 is associated with neurodegenerative disorders, such as Alzheimer’s disease, Parkinson’s disease, and ataxias, where impaired protein degradation leads to the accumulation of toxic protein aggregates. Knockout studies reveal increased protein misfolding, cellular stress, and neurodegeneration, highlighting its essential role in maintaining proteome integrity and cellular homeostasis.