SRSF10 (serine and arginine rich splicing factor 10) is an atypical SR protein that functions as a context-dependent regulator of pre-mRNA alternative splicing 1. In its dephosphorylated state, SRSF10 acts as a general splicing repressor by interfering with U1 snRNP recognition and promoting exon skipping during alternative splicing 2. The protein's activity is tightly regulated by phosphorylation, particularly by CK1ε kinase at residues S23 and S133, which modulates its RNA-binding capacity and splicing regulatory function 3. SRSF10 expression is uniquely controlled through an autoregulated minor intron, creating tight correlation with minor spliceosome abundance across tissues and establishing crosstalk between minor and major splicing pathways 4. Beyond splicing regulation, SRSF10 plays critical roles in cancer biology by stabilizing oncogenic transcripts like MYB, promoting glycolysis and lactate production that drives M2 macrophage polarization and immune evasion in hepatocellular carcinoma 5. The protein also regulates apoptotic balance by controlling Bcl-x alternative splicing, favoring anti-apoptotic Bcl-xL production 3, and influences glioma cell metabolism through the SNORD46/FTSJ3/FOXO4 pathway 6. Given its oncogenic roles, SRSF10 represents a promising therapeutic target, with small molecule inhibitors showing efficacy in colorectal cancer models 7.