SRSF protein kinase 2

SRPK2 (serine/arginine-rich protein kinase 2) is a serine kinase that phosphorylates SR splicing factors at arginine/serine-rich (RS) domains and regulates pre-mRNA splicing, spliceosomal assembly, and neuronal apoptosis (UniProt: P78362). The protein modulates splicing factor activity through phosphorylation of substrates including SRSF2 and DDX23, and can influence cyclin-D1 expression and apoptotic pathways in neurons. UniProt records no primary disease associations for SRPK2.

In Alzheimer's disease, SRPK2 is significantly downregulated in post-mortem AD brain tissue compared to age-matched controls, with a mean log2 fold-change of −0.47 (Chaparral AD proteomics). This downregulation was detected via TMT-labeled quantitative proteomics across subcellular fractions from AD brain samples. The reduced abundance of this splicing kinase in AD pathology may have implications for altered RNA processing and neuronal viability, though the specific functional consequences in the disease context require further investigation.