The biology of DHX9 and its potential as a therapeutic target
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Teresa Lee1 and Jerry Pelletier1,2,3
1 Department of Biochemistry, McGill University, Montreal, Quebec, Canada
2 Department of Oncology, McGill University, Montreal, Quebec, Canada
3 Department of Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, Quebec, Canada
Jerry Pelletier, email:
Keywords: DHX9, helicase, RNA helicase A, DExD/H-box, Maleless
Received: February 09, 2016 Accepted: March 16, 2016 Published: March 28, 2016
DHX9 is member of the DExD/H-box family of helicases with a “DEIH” sequence at its eponymous DExH-box motif. Initially purified from human and bovine cells and identified as a homologue of the Drosophila Maleless (MLE) protein, it is an NTP-dependent helicase consisting of a conserved helicase core domain, two double-stranded RNA-binding domains at the N-terminus, and a nuclear transport domain and a single-stranded DNA-binding RGG-box at the C-terminus. With an ability to unwind DNA and RNA duplexes, as well as more complex nucleic acid structures, DHX9 appears to play a central role in many cellular processes. Its functions include regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. Because of its central role in gene regulation and RNA metabolism, there are growing implications for DHX9 in human diseases and their treatment. This review will provide an overview of the structure, biochemistry, and biology of DHX9, its role in cancer and other human diseases, and the possibility of targeting DHX9 in chemotherapy.
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