TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase

被引:58
作者
Urano, Tomohiko [1 ,2 ,3 ]
Usui, Takahiko [1 ,2 ]
Takeda, Shizu [4 ]
Ikeda, Kazuhiro [3 ]
Okada, Atsushi [1 ,2 ]
Ishida, Yoshiko [4 ]
Iwayanagi, Takao [4 ,5 ]
Otomo, Jun [4 ]
Ouchi, Yasuyoshi [1 ]
Inoue, Satoshi [1 ,2 ,3 ]
机构
[1] Univ Tokyo, Grad Sch Med, Dept Geriatr Med, Bunkyo Ku, Tokyo 1138655, Japan
[2] Univ Tokyo, Grad Sch Med, Dept Antiaging Med, Bunkyo Ku, Tokyo 1138655, Japan
[3] Saitama Med Sch, Res Ctr Genom Med, Hidaka, Saitama 3501241, Japan
[4] Hitachi Ltd, Cent Res Lab, Kokubunji, Tokyo 1858601, Japan
[5] Natl Inst Genet, Lab Res & Dev Biol Database, Mishima, Shizuoka 4118540, Japan
关键词
TRIM44; Terf; RING finger; E3 ubiquitin ligase; LINDAU TUMOR-SUPPRESSOR; PROTEIN; IDENTIFICATION; DEGRADATION; DEUBIQUITINATION; MECHANISMS; MID1; RO52;
D O I
10.1016/j.bbrc.2009.04.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Terf/TRIM17 is a member of the TRIM family of proteins, which is characterized by the RING finger, B-box, and coiled-coil domains. In the present Study, we found that terf interacts with TRIM44. Terf underwent ubiquitination in vitro in the presence of the E2 enzyme UbcH6; this Suggests that terf exhibits E3 ubiquitin ligase activity. It was also found that terf was conjugated with polyubiquitin chains and stabilized by the proteasome inhibitor in mammalian cells: this Suggested that terf tendered itself susceptible to proteasomal degradation through polyubiquitination. We also found that TRIM44 inhibited ubiquitination of terf, and thus stabilized the protein. The N-terminal region of TRIM44 contains a zinc-finger domain found in ubiquitin hydrolases (ZF UBP) and ubiquitin specific proteases (USPs). Thus, we proposed that TRIM44 may function as a new class of the "USP-like-TRIM" which regulates the activity of associated TRIM proteins. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:263 / 268
页数:6
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