TRIM8 regulates Nanog via Hsp90β-mediated nuclear translocation of STAT3 in embryonic stem cells.
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.
Mesh Terms:
Active Transport, Cell Nucleus, Animals, CHO Cells, Carrier Proteins, Cell Nucleus, Cells, Cultured, Cricetinae, Cricetulus, Embryonic Stem Cells, Gene Expression Regulation, Developmental, HSP90 Heat-Shock Proteins, HeLa Cells, Homeodomain Proteins, Humans, Mice, Models, Biological, Nerve Tissue Proteins, Phosphorylation, Protein Binding, Protein Transport, RNA, Small Interfering, STAT3 Transcription Factor
Active Transport, Cell Nucleus, Animals, CHO Cells, Carrier Proteins, Cell Nucleus, Cells, Cultured, Cricetinae, Cricetulus, Embryonic Stem Cells, Gene Expression Regulation, Developmental, HSP90 Heat-Shock Proteins, HeLa Cells, Homeodomain Proteins, Humans, Mice, Models, Biological, Nerve Tissue Proteins, Phosphorylation, Protein Binding, Protein Transport, RNA, Small Interfering, STAT3 Transcription Factor
Biochim. Biophys. Acta
Date: Oct. 01, 2011
PubMed ID: 21689689
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