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TAB2, an important upstream adaptor of interleukin-1 signaling pathway, is subject to SUMOylation

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Abstract

SUMOylation has been considered as an important mechanism to regulate multiple cellular processes, including inflammation. TAB2 (TAK1-binding protein 2) is an upstream adaptor protein in the IL-1 signaling pathway. Covalent modifications of TAB2 have not been well studied. In this study, we demonstrated that TAB2 could be modified by SUMO. Using Ubc9 (SUMO-conjugating enzyme) fusion and mutation analysis, we identified evolutionarily conserved lysine 329 as the major SUMOylation site of TAB2. PIAS3, a SUMO E3 ligase, preferentially interacted with and promoted its SUMOylation. Interestingly, block of SUMOylation by mutation of lysine 329 enhanced the activity of TAB2, as reflected by AP-1 luciferase reporter assays. Taken together, these results suggest that SUMOylation may serve as a novel mechanism for the regulation of TAB2.

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Acknowledgments

We are grateful to Imelda Lee from Shanghai Clinical Center for Endocrine and Metabolic Diseases for critical readings. This study was supported by the Grants from National Natural Science Foundation of China (No. 30871203 and No. 30900702), Shanghai Committee for Science and Technology (No. 08DZ2271000), and Shanghai Municipal Natural Science Foundation (No. 09ZR1427600).

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Authors and Affiliations

  1. Shanghai Clinical Center for Endocrine and Metabolic Diseases, Shanghai Institute of Endocrinology and Metabolism, School of Medicine, Ruijin Hospital, Shanghai Jiao Tong University, Shanghai, 200025, China

    Xiaolin Wang, Jingjing Jiang, Yan Lu, Guojun Shi, Ruixin Liu & Yanan Cao

  2. The Key Laboratory of Endocrine Tumors and the Division of Endocrine and Metabolic Diseases, E-Institute of Shanghai Universities, Shanghai, 200025, China

    Yan Lu, Guojun Shi, Ruixin Liu & Yanan Cao

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  1. Xiaolin Wang
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  2. Jingjing Jiang
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Correspondence to Yanan Cao.

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Wang, X., Jiang, J., Lu, Y. et al. TAB2, an important upstream adaptor of interleukin-1 signaling pathway, is subject to SUMOylation. Mol Cell Biochem 385, 69–77 (2014). https://doi.org/10.1007/s11010-013-1815-3

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  • DOI: https://doi.org/10.1007/s11010-013-1815-3

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