SRSF6 (serine and arginine rich splicing factor 6) is a critical regulator of alternative mRNA splicing that controls constitutive and alternative splice site selection. The protein functions by binding to specific RNA motifs and recruiting other splicing factors to modulate exon inclusion or exclusion 12. SRSF6 operates through its RNA recognition motif domains, particularly the RRM2 domain, to directly bind target transcripts and regulate their splicing patterns 1. The protein cooperates with other splicing regulators including SRSF1, HNRNPC, and USP39 to orchestrate complex splicing programs 23. SRSF6 is subject to posttranslational regulation, including phosphorylation by SRPK1 and stabilization through USP7-mediated deubiquitination 45. In disease contexts, SRSF6 is frequently upregulated in cancers including colorectal cancer, prostate cancer, and thyroid carcinoma, where it promotes oncogenic splicing programs that enhance tumor progression, metastasis, and drug resistance 167. SRSF6 also plays roles in metabolic diseases like NAFLD/NASH through regulation of mitochondrial function-related gene splicing 4. The protein's critical role in cellular survival and disease progression makes it an attractive therapeutic target, with several inhibitors showing promise in preclinical studies 15.