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TRIM11 binds to and destabilizes a key component of the activator‐mediated cofactor complex (ARC105) through the ubiquitin–proteasome system
Author(s) -
Ishikawa Hideaki,
Tachikawa Hiroyuki,
Miura Yutaka,
Takahashi Nobuhiro
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.066
Subject(s) - ubiquitin , activator (genetics) , proteasome , transcription factor , microbiology and biotechnology , signal transduction , cofactor , chemistry , biology , biochemistry , enzyme , gene
TRIM11 is a member of the tripartite‐motif‐containing protein family and is known to destabilize humanin, an inhibitor of Alzheimer‐like neuronal insults. In this study, we demonstrate that TRIM11 interacts with activator‐recruited cofactor 105‐kDa component (ARC105) that mediates chromatin‐directed transcription activation and is a key regulatory factor for transforming growth factor β (TGFβ) signaling. Co‐expression of TRIM11 increased ARC105 degradation but a proteasome inhibitor suppressed this. Co‐expression of TRIM11 and ARC105 also increased ubiquitination of ARC105. In addition, TRIM11 suppressed ARC105‐mediated transcriptional activation induced with TGFβ in a reporter assay. These results suggest that TRIM11, with the ubiquitin–proteasome pathway, regulates ARC105 function in TGFβ signaling.