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TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase |
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| Authors: | Tomohiko Urano Takahiko Usui Shizu Takeda Atsushi Okada Yoshiko Ishida Jun Otomo Satoshi Inoue |
| Affiliation: | a Department of Geriatric Medicine, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan b Department of Anti-Aging Medicine, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan c Research Center for Genomic Medicine, Saitama Medical School, 1397-1, Yamane, Hidaka-shi, Saitama 350-1241, Japan d Central Research Laboratory, Hitachi, Ltd., 1-280, Higashi-Koigakubo, Kokubunji-shi, Tokyo 185-8601, Japan e Laboratory for the Research and Development of Biological Databases, National Institute of Genetics, Yata, Mishima 411-8540, Japan |
| Abstract: | 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. |
| Keywords: | TRIM44 Terf RING finger E3 ubiquitin ligase |
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