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DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs [RNA-Seq cervical]

GSE252326 Homo sapiens Expression profiling by high throughput sequencing 6 samples Submitted 2024/12/04 Platform GPL24676
Summary
Glucose, traditionally recognized as a primary energy source, has recently emerged as a key regulator of protein interactions, particularly when intracellular glucose levels increase during cellular differentiation. Recent research has unveiled the intriguing phenomenon of glucose binding to a variety of proteins. Here, we focus on DDX50, a pivotal RNA helicase with a crucial role in epidermal differentiation. The interaction between glucose and the ATP-binding domain of DDX50 induces a significant change in the protein's conformation, resulting in the dissociation of DDX50 dimers. In the context of cellular differentiation, the increase in glucose levels promotes the formation of a complex involving DDX50, RNA, and STAU1. This complex, in turn, influences RNA structures and functions as a stabilizing force for the mRNA of key pro-differentiation genes. These genes include TINCR, OVOL1, CEBPB, PRDM1 and JUN. These findings reveal a previously unrecognized mechanism by which glucose exerts its influence, demonstrating its remarkable capacity to modulate the dimerization and function of the RNA helicase DDX50, which plays a critical role in tissue differentiation.
Published in
DDX50 cooperates with STAU1 to effect stabilization of pro-differentiation RNAs
Miao W, Porter DF, Siprashvili Z et al. · Cell reports 2025 · PMID 39764852 · doi:10.1016/j.celrep.2024.115174
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Also filed as BioProject PRJNA1059643 and SRA study SRP480826. Searching any of these in the dataset finder brings you back here.

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