| Description |
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.
Overall design: 24 samples of in vitro DMS probing data against total RNA from keratinocytes, with no DMS control, BSA control, glucose, or other proteins added.
***Raw data have been deposited in dbGaP (phs003766.v1.p1)*** |
