SRPK2 is a serine/arginine-rich protein kinase that phosphorylates SR splicing factors at RS domains, regulating pre-mRNA splicing and spliceosomal B complex formation 1. Beyond splicing, SRPK2 functions as a metabolic regulator and oncogenic driver with diverse pathological implications. In lipid metabolism, SRPK2 operates downstream of mTORC1 to phosphorylate SRSF1, coupling transcription and splicing of lipogenic enzymes through the FAM120A-SREBP1 complex 2. This function is pathologically relevant in alcohol-associated liver disease, where SRPK2 activation promotes lipogenesis via altered splicing of lipin 1 and SREBP1, and inhibition by FGF21 ameliorates disease progression 3. Similarly, in osteosarcoma, SRPK2 regulates ACSL3 splicing to influence ferroptosis susceptibility through lipid metabolism 4. In cancer, SRPK2 promotes tumorigenesis across multiple malignancies. In colorectal cancer, SRPK2 drives migration, invasion, and chemoresistance via SRPK2-Numb-p53 signaling, negatively regulating wild-type p53 5. SRPK2 activates ERK signaling in colon cancer growth and migration 6. In hepatocellular carcinoma, LINC01446 activates SRPK2-SRSF1 axis to promote VEGFA165 splicing, enhancing angiogenesis and proliferation 7. In obesity-associated pancreatic cancer, SRPK2 drives stress granule formation downstream of mTOR/S6K1 hyperactivation 8. These findings establish SRPK2 as a therapeutic target in metabolic and malignant diseases.