SRPK1 (serine/arginine-rich protein kinase 1) is a multifunctional protein kinase that phosphorylates SR splicing factors at serine residues within RS domains, serving as a central regulator of pre-mRNA splicing and nuclear organization [UniProt]. Beyond splicing, SRPK1 catalyzes phosphorylation of diverse substrates including protamines during parental genome reprogramming in fertilized oocytes, initiating protamine-to-histone exchange essential for early embryonic development 1. SRPK1 exhibits spatiotemporal expression patterns throughout brain development with coexpression linked to neurodevelopmental processes 2. In disease contexts, SRPK1 becomes pathologically upregulated: in lung adenocarcinoma, METTL3-mediated m6A methylation stabilizes SRPK1, which then promotes glycolysis through PKM2 splicing regulation 3. SRPK1 expression is elevated in intracranial aneurysms, where its silencing reduces VSMC apoptosis and promotes pathological vascular remodeling via PI3K/Akt inhibition 4. In hepatic steatosis, SRPK1 activity is inhibited by DRAK2 binding, reducing splicing factor SRSF6 phosphorylation and suppressing NAFLD progression 5. Additionally, SRPK1 undergoes S-palmitoylation and ubiquitin-dependent degradation in high-fat conditions, modulating p53-dependent ferroptosis in endothelial dysfunction 6. These findings position SRPK1 as both essential for normal cellular processes and a therapeutic target in multiple pathological conditions.