SAF-A/hnRNP U binds polyphosphoinositides via a lysine rich polybasic motif located in the SAP domain.

Autor:	Edson AJ; Department of Biological Sciences, University of Bergen, Bergen, Vestland, Norway., Jacobsen RG; Department of Biological Sciences, University of Bergen, Bergen, Vestland, Norway., Lewis AE; Department of Biological Sciences, University of Bergen, Bergen, Vestland, Norway.
Jazyk:	angličtina
Zdroj:	MicroPublication biology [MicroPubl Biol] 2023 Mar 24; Vol. 2023. Date of Electronic Publication: 2023 Mar 24 (Print Publication: 2023).
DOI:	10.17912/micropub.biology.000761
Abstrakt:	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. (Copyright: © 2023 by the authors.)
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu