Pre-mRNA-splicing factor SLU7 (SLU7)

Pre-mRNA-splicing factor SLU7 (SLU7) is a highly conserved splicing factor essential for the second catalytic step of pre-mRNA splicing in the nucleus. SLU7 is a component of the spliceosome complex, particularly recruited during the transition to the catalytic C* complex, where it plays a critical role in selecting the 3′ splice site and enabling exon ligation in mRNA maturation. The human SLU7 protein contains a conserved zinc knuckle motif, nuclear localization signal, leucine-rich regions, and a lysine-rich domain, which together regulate its localization and function in splicing. Beyond its canonical splicing role, SLU7 participates in broader gene expression regulation, including transcriptional modulation, DNA methylation, and protein stability. Deficiencies or mutations in SLU7 impact genome integrity and have been associated with R-loop formation, DNA damage, cell-cycle arrest, and mitotic defects. Altered SLU7 function is implicated in cancer, especially liver cancer (hepatocarcinogenesis), through its effects on splicing of specific oncogenic factors such as SRSF3. SLU7 is currently not a direct therapeutic target, and no drugs are known to act upon it[1][2][3][4].

Other names

hSlu7SLU7 homologsplicing factor SLU7step II splicing factor SLU7spliceosome associated SLU7zinc knuckle motif containingpre-mRNA-splicing factor SLU7