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We recently reported that diadenosine tetraphosphate hydrolase (Ap4 A hydrolase) plays a critical role in gene expression via regulation of intracellular Ap4 A levels. This enzyme serves as a component of our newly described lysyl tRNA synthetase (LysRS)-Ap4 A biochemical pathway that is triggered upon immunological challenge. Here we explored the mechanism of this enzyme's translocation into the nucleus and found its immunologically dependent association with importin beta. Silencing of importin beta prevented Ap4 A hydrolase nuclear translocation and affected the local concentration of Ap4 A, which led to an increase in microphthalmia transcription factor (MITF) transcriptional activity. Furthermore, immunological activation of mast cells resulted in dephosphorylation of Ap4 A hydrolase, which changed the hydrolytic activity of the enzyme.

Importin Beta Plays an Essential Role in the Regulation of the LysRS-Ap4A Pathway in Immunologically Activated Mast Cells

Importin Beta Plays an Essential Role in the Regulation of the LysRS-Ap₄A Pathway in Immunologically Activated Mast Cells