TRIM8 modulates STAT3 activity through negative regulation of PIAS3.
TRIM8 is a member of the protein family defined by the presence of a common domain structure composed of a tripartite motif: a RING-finger, one or two B-box domains and a coiled-coil motif. Here, we show that TRIM8 interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation ... of STAT3. Ectopic expression of TRIM8 cancels the negative effect of PIAS3 on STAT3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus. Furthermore, expression of TRIM8 in NIH3T3 cells enhances Src-dependent tumorigenesis. These findings indicate that TRIM8 enhances the STAT3-dependent signal pathway by inhibiting the function of PIAS3.
Mesh Terms:
Animals, Carrier Proteins, HeLa Cells, Humans, Interleukin-6, Mice, Molecular Chaperones, NIH 3T3 Cells, Nerve Tissue Proteins, Protein Inhibitors of Activated STAT, STAT3 Transcription Factor, Signal Transduction, Transcription, Genetic, Two-Hybrid System Techniques, Ubiquitination, src-Family Kinases
Animals, Carrier Proteins, HeLa Cells, Humans, Interleukin-6, Mice, Molecular Chaperones, NIH 3T3 Cells, Nerve Tissue Proteins, Protein Inhibitors of Activated STAT, STAT3 Transcription Factor, Signal Transduction, Transcription, Genetic, Two-Hybrid System Techniques, Ubiquitination, src-Family Kinases
J. Cell. Sci.
Date: Jul. 01, 2010
PubMed ID: 20516148
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