Article

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

Department of Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo, Hokkaido 060-8638, Japan.
Biochimica et Biophysica Acta (impact factor: 4.66). 06/2011; 1813(10):1784-92. DOI:10.1016/j.bbamcr.2011.05.013 pp.1784-92
Source: PubMed

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.

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Keywords

B-box domains
 
common domain structure
 
interacts
 
nucleus
 
phosphorylated STAT3
 
protein family
 
RING-finger
 
selectively downregulates transcription
 
STAT3
 
TRIM8 interacts
 
TRIM8 modulates translocation
 
tripartite motif