Proteomic study identifies Aurora-A-mediated regulation of alternative splicing through multiple splicing factors.

ABSTRACT: The cell cycle regulator Aurora-A kinase presents an attractive target for cancer therapies, though its inhibition is also associated with toxic side effects. To gain a more nuanced understanding of Aurora-A function, we applied shotgun proteomics to identify 407 specific protein partners, including several splicing factors. Supporting a role in alternative splicing, we found that Aurora-A localizes to nuclear speckles, the storehouse of splicing proteins. Aurora-A interacts with and phosphorylates splicing factors both in vitro and in vivo, suggesting that it regulates alternative splicing by modulating the activity of these splicing factors. Consistently, Aurora-A inhibition significantly impacts the alternative splicing of 505 genes, with RNA motif analysis revealing an enrichment for A

SUBMITTER: Damodaran AP 

PROVIDER: S-EPMC11732490 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature