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SUMO E3 ligase activity of TRIM proteins

Oncogene volume 30, pages 1108–1116 (2011)Cite this article

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Abstract

SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins.

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Acknowledgements

We thank Dr PP Pandolfi for providing Pml−/− MEF cells and Drs V Yu, A-M Herr, F Rauscher III and TC Cox for TRIM-expressing plasmids. We also thank E Fischer and S Slattery for technical assistance and A Stonestrom for help with manuscript preparation. Supported by NIH (CA088868 and GM060911) to XY.

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  1. Y Chu

    Present address: 2Current address: Department of Pediatrics, Columbia University, New York, NY, USA.,

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  1. Department of Cancer Biology and Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, USA

    Y Chu & X Yang

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Correspondence to X Yang.

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Chu, Y., Yang, X. SUMO E3 ligase activity of TRIM proteins. Oncogene 30, 1108–1116 (2011). https://doi.org/10.1038/onc.2010.462

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