Nuclear termination of STAT3 signaling through SIPAR (STAT3-Interacting Protein As a Repressor)-dependent recruitment of T cell tyrosine phosphatase TC-PTP.

is associated with embryo development and survival as well as proliferation and metastasis of tumor cells. In a previous study, we demonstrated that Protein As a Repressor (SIPAR) enhances the dephosphorylation of duanyu18133 and negatively regulates its activity. However, it remains unclear how SIPAR inhibits phosphorylation of Here we demonstrate that SIPAR directly interacts with T cell protein tyrosine phosphatase TC45 and enhances its association with duanyu18133. This interaction triggers an accelerated dephosphorylation process for duanyu18133. Furthermore, SIPAR inhibits the transcriptional activity of duanyu18133 in wild-type MEF cells but not in TC45 null MEF cells. These results suggest that SIPAR terminates the activation of duanyu18133 through a dephosphorylation process that is dependent upon interaction with TC45 in the nucleus.

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