Heat shock protein HSP 90-alpha

Heat shock protein HSP90-alpha (HSP90AA1) is a molecular chaperone that promotes maturation, structural maintenance, and proper regulation of target proteins involved in cell cycle control and signal transduction (UniProt: P07900). It functions through an ATP-dependent cycle that facilitates client protein folding and activation, while also interacting with co-chaperones that modulate substrate recognition and chaperone activity. Beyond its canonical chaperone role, HSP90-alpha regulates transcription machinery through modification of transcription factor levels, epigenetic modifiers, and histone positioning, and mediates inflammatory and antiviral responses via LPS binding and mitochondrial signaling.

HSP90-alpha is widely expressed and contributes to multiple cellular pathways including protein homeostasis, mitochondrial protein import, and innate immune signaling (UniProt: P07900). No primary UniProt disease annotations are recorded for this protein.

HSP90-alpha is curated as relevant to Alzheimer's Disease in this dataset. Evidence from human post-mortem AD brain proteomics shows direction is ambiguous across subcellular fractions, with a mean log2 fold-change of 0.0712 relative to age-matched controls (Chaparral AD proteomics). This minimal average change masks differential regulation across cellular compartments, suggesting context-dependent involvement in AD pathology.