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

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• 作者：Tomohiko Urano ; Takahiko Usui ; Shizu Takeda ; Kazuhiro Ikeda ; Atsushi Okada ; Yoshiko Ishida ; Takao Iwayanagi ; Jun Otomo ; Yasuyoshi Ouchi ; Satoshi Inoue
• 关键词：TRIM44 ; Terf ; RING finger ; E3 ubiquitin ligase
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2009
• 出版时间：29 May 2009
• 年：2009
• 卷：383
• 期：2
• 页码：263-268
• 全文大小：383 K

文摘

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 rendered 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.