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Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.

ABSTRACT: 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.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.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.

SUBMITTER: Liu X

PROVIDER: S-EPMC3048563 | biostudies-other | 2011 Feb

REPOSITORIES: biostudies-other

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Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.

Liu Xinlei X Lei Xiaobo X Zhou Zhuo Z Sun Zhenmin Z Xue Qinghua Q Wang Jianwei J Hung Tao T

Virology journal 20110210

<h4>Background</h4>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.<h4>Results</h4>Our study shows that, similar to other TRIM family members, TRIM38 is ...[more]

PMID: 21306652

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