TRIM8 regulates Nanog via Hsp90β-mediated nuclear translocation of STAT3 in embryonic stem cells

Fumihiko Okumura, Akiko J. Okumura, Masaki Matsumoto, Keiichi I. Nakayama, Shigetsugu Hatakeyama

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

Abstract

TRIM8 is a member of a protein family defined by the presence of a common domain structure composed of a tripartite motif including a RING-finger, one or two B-box domains and a coiled-coil motif. Here, we show that TRIM8 interacts with Hsp90β, which interacts with STAT3 and selectively downregulates transcription of Nanog in embryonic stem cells. Knock-down of TRIM8 increased phosphorylated STAT3 in the nucleus and also enhanced transcription of Nanog. These findings suggest that TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90β and consequently regulates transcription of Nanog in embryonic stem cells.

Original languageEnglish
Pages (from-to)1784-1792
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1813
Issue number10
DOIs
Publication statusPublished - Oct 2011

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'TRIM8 regulates Nanog via Hsp90β-mediated nuclear translocation of STAT3 in embryonic stem cells'. Together they form a unique fingerprint.

Cite this