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Biochem Biophys Res Commun. 2009 May 29;383(2):263-8. doi: 10.1016/j.bbrc.2009.04.010. Epub 2009 Apr 7.

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

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  • 1Department of Geriatric Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, 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.

PMID:
19358823
DOI:
10.1016/j.bbrc.2009.04.010
[PubMed - indexed for MEDLINE]
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