Abstract
Much interest has been expended lately in characterizing the association between DExH-Box helicase 9 (DHX9) dysregulation and malignant development, however, the enigmatic nature of DHX9 has caused conflict as to whether it regularly functions as an oncogene or tumor suppressor. The impact of DHX9 on malignancy appears to be cell-type specific, dependent upon the availability of binding partners and activation of inter-connected signaling pathways. Realization of DHX9’s pivotal role in the development of several hallmarks of cancer has boosted the enzyme's potential as a cancer biomarker and therapeutic target, opening up novel avenues for exploring DHX9 in precision medicine applications. Our review discusses the ascribed functions of DHX9 in cancer, explores its enigmatic nature and potential as an antineoplastic target.
Highlights
Amino acidMetabolism via remodeling ribonucleoprotein complexes, processing pre-mRNA and catalyzing ribosomal RNA biogenesis [10,11]
R Hoffmann was responsible for the review, editing and final approval of the manuscript publishing
Summary
Metabolism via remodeling ribonucleoprotein complexes, processing pre-mRNA and catalyzing ribosomal RNA biogenesis [10,11]. DHX9 is an abundant, nuclear protein with a variety of putative roles including maintenance of genomic stability, DNA replication, transcription and translation [15] It shuttles between the nucleus and cytoplasm and is capable of binding both ssDNA and ssRNA, as well as unwinding double-stranded (ds) nucleic acids and complex polynucleotide structures. DNA replication The aforementioned role of DXH9 in the resolution of transcription/replication conflicts prevents replication stress by allowing the replication machinery to function efficiently (Figure 2B) and this highlights a role for DHX9 in regulation of DNA replication [30] Consistent with this notion, DHX9 binds to, and enhances the activity of, an enzyme called WRN helicase that is involved in both DNA replication and the maintenance of genomic integrity [32,33]. DHX9 regulates translational efficiency via binding and unwinding rG4 structures to stimulate the future science group mRNA
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