[No authors listed]
Since cancer is the leading cause of death worldwide, there is an urgent need to understand the mechanisms underlying cancer progression and the development of cancer inhibitors. Signal transducer and activator of transcription 3 is a major transcription factor that regulates the proliferation and survival of various cancer cells. Here, dual-specificity phosphatase 3 (DUSP3) was identified as a regulator of based on an interaction screening performed using the protein tyrosine phosphatase library. DUSP3 interacted with the C-terminal domain of duanyu18133 and dephosphorylated p-Y705 of In vitro dephosphorylation assay revealed that DUSP3 directly dephosphorylated The suppressive effects of DUSP3 on duanyu18133 were evaluated by a decreased promoter activity, which in turn reduced the expression of the downstream target genes of duanyu18133. In summary, DUSP3 downregulated the transcriptional activity of duanyu18133 via dephosphorylation at Y705 and also suppressed the migratory activity of cancer cells. This study demonstrated that DUSP3 inhibits interleukin 6 signaling and is expected to regulate cancer development. Novel functions of DUSP3 discovered in signaling regulation would help expand the understanding of cancer development mechanisms.
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