Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2238-2245 |
| Number of pages | 8 |
| Journal | Journal of Cell Science |
| Volume | 123 |
| Issue number | 13 |
| DOIs | |
| Publication status | Published - Jul 1 2010 |
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All Science Journal Classification (ASJC) codes
- Cell Biology
- Medicine(all)
Cite this
TRIM8 modulates STAT3 activity through negative regulation of PIAS3. / Okumura, Fumihiko; Matsunaga, Yui; Katayama, Yuta; Nakayama, Keiichi; Hatakeyama, Shigetsugu.
In: Journal of Cell Science, Vol. 123, No. 13, 01.07.2010, p. 2238-2245.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - TRIM8 modulates STAT3 activity through negative regulation of PIAS3
AU - Okumura, Fumihiko
AU - Matsunaga, Yui
AU - Katayama, Yuta
AU - Nakayama, Keiichi
AU - Hatakeyama, Shigetsugu
PY - 2010/7/1
Y1 - 2010/7/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77954364837&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77954364837&partnerID=8YFLogxK
U2 - 10.1242/jcs.068981
DO - 10.1242/jcs.068981
M3 - Article
VL - 123
SP - 2238
EP - 2245
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 13
ER -