SLU7 is a multifunctional spliceosomal protein essential for pre-mRNA splicing and broader gene expression regulation. As a core component of the spliceosome, SLU7 participates in the second catalytic step of splicing, facilitating the attack of the free 3'-hydroxyl group on exon 1 at the 3'-splice site to generate spliced mRNA 1. SLU7 adopts an extended conformation binding to Prp8 and Cwc22, positioning itself for accurate 3'-splice site selection, particularly when multiple potential sites exist 1. Beyond splicing, SLU7 functions as an integrative hub regulating multiple gene expression levels, including epigenetic DNA remodeling through DNMT1 stabilization and DNA methylation maintenance 2, and modulation of protein stability 3. Clinically, SLU7 dysregulation associates with cancer development and progression. Aberrant SLU7 expression contributes to hepatocellular carcinogenesis through caspase-mediated degradation during liver injury, which impairs nonsense-mediated mRNA decay (NMD) by destabilizing the NMD effector UPF1 4. In bladder cancer, SLU7 complexes with G3BP1 to promote immune evasion by downregulating MHC-I via PI3K/Akt signaling 5. SLU7 is conversely essential for cancer cell survival; its knockdown induces genomic instability, DNA damage, and enhanced immunogenicity 6. These findings position SLU7 as a promising dual-action therapeutic target combining direct tumor suppression with immune activation 6.