TRIM8 modulates STAT3 activity through negative regulation of PIAS3

Fumihiko Okumura, Yui Matsunaga, Yuta Katayama, Keiichi Nakayama, Shigetsugu Hatakeyama

Research output: Contribution to journalArticle

40 Citations (Scopus)

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 languageEnglish
Pages (from-to)2238-2245
Number of pages8
JournalJournal of Cell Science
Volume123
Issue number13
DOIs
Publication statusPublished - Jul 1 2010

Fingerprint

Proteins
RING Finger Domains
Proteasome Endopeptidase Complex
Ubiquitin
Proteolysis
Interleukin-6
Signal Transduction
Carcinogenesis
Ectopic Gene Expression

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 journalArticle

Okumura, Fumihiko ; Matsunaga, Yui ; Katayama, Yuta ; Nakayama, Keiichi ; Hatakeyama, Shigetsugu. / TRIM8 modulates STAT3 activity through negative regulation of PIAS3. In: Journal of Cell Science. 2010 ; Vol. 123, No. 13. pp. 2238-2245.
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