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- Title
TAB2, an important upstream adaptor of interleukin-1 signaling pathway, is subject to SUMOylation.
- Authors
Wang, Xiaolin; Jiang, Jingjing; Lu, Yan; Shi, Guojun; Liu, Ruixin; Cao, Yanan
- 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.
- Publication
Molecular and cellular biochemistry, 2014, Vol 385, Issue 1-2, p69
- ISSN
1573-4919
- Publication type
Journal Article
- DOI
10.1007/s11010-013-1815-3