Journal
JOURNAL OF CELL SCIENCE
Volume 123, Issue 13, Pages 2238-2245Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.068981
Keywords
TRIM8; PIAS3; Ubiquitin; STAT3; IL-6
Categories
Funding
- Ministry of Education, Culture, Sports, Science and Technology
- Mitsubishi Pharma
- Cell Science Research Foundation
- Research Foundation Ituu Laboratory
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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.
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