LSM7 is an RNA-binding protein that functions as a core component of the spliceosome, specifically within the U4/U6-U5 tri-snRNP complex and the heptameric LSM2-8 complex, where it binds the 3'-terminal U-tract of U6 snRNA to facilitate pre-mRNA splicing. Beyond splicing, LSM7 participates in mRNA decay and stress granule formation, processes regulated through liquid-liquid phase separation. In breast cancer, LSM7 is significantly overexpressed in metastatic tissues and drives metastasis by mediating alternative splicing of CD44 to produce the CD44s isoform, enhancing cell migration and invasion 1. Similarly, in hepatocellular carcinoma, elevated LSM7 expression correlates with adverse clinicopathological features and poor prognosis, and associates with immune evasion through altered immune cell infiltration and upregulated immune checkpoints 2. In non-small cell lung cancer, LSM7 suppresses tumor progression and increases immune infiltration, showing synergistic effects with anti-PD-1 therapy 3. Biallelic LSM7 variants cause defective assembly of LSM complexes and impair neurodevelopment, implicating the gene in leukodystrophies 4. Rare variant burden studies suggest LSM7 involvement in Parkinson's disease 5. Velpatasvir has been identified as a candidate LSM7-targeting agent in hepatocellular carcinoma.