SAF-A/hnRNP U binds polyphosphoinositides via a lysine rich polybasic motif located in the SAP domain
Journal article, Peer reviewed
Published version
![Thumbnail](/bora-xmlui/bitstream/handle/11250/3066362/2023%2bmicropub-biology-SAF-A%2bhnRNP%2bU%2bbinds%2bpolyphosphoinositides%2bvia%2ba%2blysine%2brich%2bpolybasic%2bmotif%2blocated%2bin%2bthe%2bSAP%2bdomain.pdf.jpg?sequence=6&isAllowed=y)
Åpne
Permanent lenke
https://hdl.handle.net/11250/3066362Utgivelsesdato
2023Metadata
Vis full innførselSamlinger
- Department of Biological Sciences [2279]
- Registrations from Cristin [10237]
Sammendrag
Polyphosphoinositides (PPIn) play essential functions as lipid signalling molecules and many of their functions have been elucidated in the cytoplasm. However, PPIn are also intranuclear where they contribute to chromatin remodelling, transcription and mRNA splicing. Using quantitative interactomics, we have previously identified PPIn-interacting proteins with roles in RNA processing/splicing including the heterogeneous nuclear ribonucleoprotein U (hnRNPU/SAF-A). In this study, hnRNPU was validated as a direct PPIn-interacting protein via 2 regions located in the N and C termini. Furthermore, deletion of the polybasic motif region located at aa 9-24 in its DNA binding SAP domain prevented PPIn interaction. In conclusion, these results are consistent with hnRNPU harbouring a polybasic region with dual functions in DNA and PPIn interaction.