Regulation of STAT3-mediated signaling by LMW-DSP2.

Signal transducer and activator of transcription 3 which mediates biological actions in many physiological processes, is activated by cytokines and growth factors, and has been reported to be constitutively activated in numerous cancer cells. In this study, we examined whether low molecular weight-dual specificity phosphatase two (LMW-DSP2) is involved in the regulation of the interleukin 6 (IL-6)/leukemia inhibitory factor signaling pathway. IL-6/LIF-induced LMW-DSP2 expression in murine testicular or hepatoma cell lines, while LMW-DSP2 overexpression in 293T cells suppressed IL-6-induced phosphorylation and activation of Furthermore, LMW-DSP2 suppressed the expression of IL-6-induced endogenous genes. In contrast, small-interfering RNA-mediated reduction of LMW-DSP2 expression enhanced IL-6-induced transcription. In fact, LMW-DSP2 interacted with in vivo and endogenous LMW-DSP2 bound to duanyu18133 in murine testicular GC-1 cells. These results strongly suggest that LMW-DSP2 acts as a negative regulator of the signaling pathway.

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