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Mol Cell Biochem. 2014 Jan;385(1-2):69-77. doi: 10.1007/s11010-013-1815-3. Epub 2013 Oct 6.

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

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  • 1Shanghai 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, visit-12345@hotmail.com.

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.

PMID:
24096733
[PubMed - indexed for MEDLINE]
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