U2AF2 controls alternative splicing in speckle-proximal regions in an RS domain-dependent manner - PubMed
5 hours ago
- #alternative splicing
- #U2AF2
- #nuclear speckles
- U2AF2 is crucial for 3' splice site recognition during spliceosome assembly.
- Proximity labeling reveals U2AF2's functional partners in splicing, chromatin modification, transcription, 3' end processing, and RNA methylation.
- Removal of the U2AF2 RS domain alters interactions, reduces nuclear speckle localization, and affects splicing genome-wide.
- Cassette exons flanked by short introns near speckles are most impacted by U2AF2 knockdown or RS domain removal.
- Phosphorylation sites in the U2AF2 RS domain are essential for normal splicing, indicating regulatory roles.
- Alternatively spliced transcripts accumulate near speckles, with U2AF2 enrichment but limited local concentration.
- Global U2AF2 reduction disproportionately affects splicing near nuclear speckles, highlighting spatial protein availability's role in splicing regulation.