Dihydrouridine synthase 4 like (DUS4L)

Dihydrouridine synthase 4 like (DUS4L) is a human enzyme responsible for catalyzing the formation of dihydrouridine—a modified nucleoside—in the D-loop of transfer RNAs (tRNAs), specifically at positions 20a and 20b. This post-transcriptional tRNA modification is essential for proper tRNA folding, stability, and function. DUS4L belongs to the family of flavin mononucleotide-dependent oxidoreductases and is structurally related to bacterial DUS proteins such as E. coli yhdg. It has been found upregulated in various cancers, including lung adenocarcinoma, and is associated with tumor stage and size. Experimental silencing of DUS4L by shRNA inhibits proliferation and induces apoptosis in cancer cell lines, indicating its oncogenic properties and value as a potential therapeutic target. Additionally, the DUS4L-BCAP29 fusion transcript has been implicated in cancer biology, although DUS4L itself also participates in normal and pathological cell processes such as ncRNA processing, ribosome biogenesis, and splicing. Disease associations extend to congenital glycosylation disorders and potentially osteoarthritis, but no approved drugs target DUS4L to date.

Other names

DUS4PP35tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-liketRNA-dihydrouridine synthase 4-likeprotein similar to E. coli yhdg and R. capsulatus nifR3

No drug mechanism documented for this specific target.