Background: The tripartite motif (TRIM) proteins are a family of more than 70 members in human. However, only a few of them have been well studied. The TRIM proteins contain the conserved RING, B-box, coiled-coil, and SPRY domains, most of which are involved in protein ubiquitination. TRIM38 is a member of the TRIM protein family, which we studied in more detail here as its functions are largely unknown. Results: Our study shows that, similar to other TRIM family members, TRIM38 is localized in the cytoplasm. TRIM38 increases ubiquitination of other cellular proteins and catalyzes self-ubiquitination. TRIM38 also promotes K63- and K48-linked ubiquitination of cellular proteins. An intact RING domain is important for the functions of TRIM38. In addition, enterovirus 71 infection induces TRIM38 degradation. Conclusions: Our observations demonstrate that TRIM38 has E3 ubiquitin ligase activity and can be degraded during virus infection. These findings may provide insight into innate immune signaling pathways. © 2011 Liu et al; licensee BioMed Central Ltd.
CITATION STYLE
Liu, X., Lei, X., Zhou, Z., Sun, Z., Xue, Q., Wang, J., & Hung, T. (2011). Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase. Virology Journal, 8. https://doi.org/10.1186/1743-422X-8-61
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