Serine/threonine-protein kinase 24

STK24 (serine/threonine-protein kinase 24) is a 443-amino-acid kinase that promotes apoptosis in response to stress stimuli and caspase activation (UniProt: Q9Y6E0). It regulates cell death pathways by modulating phosphorylation of stress-response kinases JNK1–JNK2 and p38 during oxidative stress, and mediates caspase-independent apoptosis through AIFM1 and ENDOG nuclear translocation. The protein also functions in cellular migration, axon regeneration, and as a component of STRIPAK complexes, which regulate Hippo, MAPK, and cytoskeleton remodeling pathways.

STK24 is broadly expressed across tissues and participates in multiple signaling networks controlling cell growth, differentiation, apoptosis, and metabolism (UniProt: Q9Y6E0). No diseases are currently annotated in UniProt for this protein.

STK24 is elevated in Alzheimer's Disease brain tissue. Chaparral AD proteomics data from human post-mortem AD brain versus age-matched controls (TMT-labeled DDA across four subcellular fractions) show STK24 is significantly upregulated with a mean log₂FC of +0.42. This upregulation may reflect enhanced apoptotic and stress-response signaling in the AD brain environment.