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Role of the SAF-A ATPase and RGG domains in X inactivation, transcription, splicing, and cell proliferation.

GSE309811 Homo sapiens Expression profiling by high throughput sequencing 6 samples Submitted 2026/02/26 Platform GPL24676
Summary
SAF-A/HNRNPU is conserved throughout vertebrates and has emerged as an important factor regulating a multitude of nuclear functions, including lncRNA localization, gene expression, and splicing. SAF-A has several functional domains, including a central ATPase domain and a C-terminal RGG domain. In this study we tested for the role of the ATP binding, ATP hydrolysis and RNA binding in X chromosome inactivation, protein dynamics, gene expression, splicing, and cell proliferation. Here we show that the ATPase and RGG domains are required to maintain XIST RNA localization and XIST-dependent histone modifications on the inactive X chromosome, to execute normal protein dynamics, and to maintain normal cell proliferation. We found that the ATPase and RGG domains are not required to maintain gene expression but play a major role in mRNA splicing. We propose a model whereby RNA binding, ATP binding and ATP hydrolysis promote SAF-A interaction with nascent RNA to promote normal mRNA splicing and XIST localization and function.
Published in
Role of the SAF-A/HNRNPU ATPase and RGG domains in X chromosome inactivation, nuclear dynamics, transcription, splicing, and cell proliferation
Sharp JA, Thomas R, Sparago E et al. · bioRxiv : the preprint server for biology 2025 · PMID 41473319 · doi:10.64898/2025.12.15.694381
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Also filed as BioProject PRJNA1363567 and SRA study SRP644353. Searching any of these in the dataset finder brings you back here.

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