Dissect c-Maf-interacting proteins and regulation of IL-10 by c-Maf
Date Issued
2008
Date
2008
Author(s)
Liu, Meng-Wei
Abstract
C-Maf is an IL-4-specific transcription factor that plays a vital role in Th2 cells differentiation. Upon stimulation, c-Maf is highly upregulated in Th2 cells as well as macrophages, and induces significant IL-4 and IL-10 expression but downregulates IL-12 expression. Thus, we hypothesized that c-Maf may have different functions through interacting with cell-specific proteins in different types of cells. Using yeast two-hybrid system, our group demonstrated that c-Maf can interact with Ubc9, the SUMOylation-specific E2 conjugating enzyme, PIAS1, the SUMOylation E3 ligase, and protein tyrosine phosphatase non-receptor type22 (PTPN22). Therefore, by Fluorescence Resonance Energy Transfer (FRET) assay, the interaction between c-Maf, Ubc9, c-Maf, PIAS1, and c-Maf, PTPN22 are confirmed. Since c-Maf can interact with SUMOylation enzymes and de-phosphorylation enzyme, which suggests that c-Maf undergoes SUMOylation and phosphorylation, these post-translational modification may affect the transactivity of c-Maf. Thereafter, we found that both c-Maf SUMOylation and phosphorylation mutants have poorer transactivity on IL-10 promoter by luciferase assay.
Subjects
c-Maf
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