Regulation of transcription factor NFAT by ADP-ribosylation
| العنوان: | Regulation of transcription factor NFAT by ADP-ribosylation |
|---|---|
| المؤلفون: | Opeyemi A. Olabisi, Xiao Yong Yang, Fernando Macian, Raymond Y L Yu, Noemi Soto-Nieves, Hee Yun Suk, Edward Nieves, Chi-Wing Chow, Teddy T.C. Yang |
| المصدر: | Molecular and cellular biology. 28(9) |
| سنة النشر: | 2008 |
| مصطلحات موضوعية: | Transcriptional Activation, T-Lymphocytes, Response element, Molecular Sequence Data, Poly (ADP-Ribose) Polymerase-1, E-box, RNA polymerase II, Biology, Mice, Sp3 transcription factor, Chlorocebus aethiops, Animals, Amino Acid Sequence, Molecular Biology, Transcription factor, Cells, Cultured, Mice, Knockout, Adenosine Diphosphate Ribose, General transcription factor, NFATC Transcription Factors, NFAT, Cell Biology, Articles, Fibroblasts, Biochemistry, biology.protein, Interleukin-2, Interleukin-4, Poly(ADP-ribose) Polymerases, Signal Transduction |
| الوصف: | ADP-ribosylation is a reversible posttranslational modification mediated by poly-ADP-ribose polymerase (PARP). The results of recent studies demonstrate that ADP-ribosylation contributes to transcription regulation. Here, we report that transcription factor NFAT binds to and is ADP-ribosylated by PARP-1 in an activation-dependent manner. Mechanistically, ADP-ribosylation increases NFAT DNA binding. Functionally, NFAT-mediated interleukin-2 (IL-2) expression was reduced in T cells upon genetic ablation or pharmacological inhibition of PARP-1. Parp-1 / T cells also exhibit reduced expression of other NFAT-dependent cytokines, such as IL-4. Together, these results demonstrate that ADP-ribosylation mediated by PARP-1 provides a molecular switch to positively regulate NFAT-dependent cytokine gene transcription. These results also imply that, similar to the effect of calcineurin inhibition, PARP-1 inhibition may be beneficial in modulating immune functions. ADP-ribosylation is a reversible posttranslational modification that transfers ADP-ribose from NAD to Glu, Asp, and/or Arg amino acids of target proteins (18). Similar to ubiquitination, ADP-ribosylation modifies target proteins to various masses due to the assorted chain lengths of the ADPribose. ADP-ribosylation is inhibited by the NAD analog 3-aminobenzamide and, more specifically, by PJ-34 (45). PolyADP-ribose polymerase-1 (PARP-1) is a nuclear enzyme that accounts for the bulk of ADP-ribosylation in vivo (43). Indeed, only 10% of PARP activity remains in Parp-1 / cells upon DNA damage. In addition to its role in DNA damage repair |
| تدمد: | 1098-5549 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::109eea886290331115232a593693af98Test https://pubmed.ncbi.nlm.nih.gov/18299389Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....109eea886290331115232a593693af98 |
| قاعدة البيانات: | OpenAIRE |
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The results of recent studies demonstrate that ADP-ribosylation contributes to transcription regulation. Here, we report that transcription factor NFAT binds to and is ADP-ribosylated by PARP-1 in an activation-dependent manner. Mechanistically, ADP-ribosylation increases NFAT DNA binding. Functionally, NFAT-mediated interleukin-2 (IL-2) expression was reduced in T cells upon genetic ablation or pharmacological inhibition of PARP-1. Parp-1 / T cells also exhibit reduced expression of other NFAT-dependent cytokines, such as IL-4. Together, these results demonstrate that ADP-ribosylation mediated by PARP-1 provides a molecular switch to positively regulate NFAT-dependent cytokine gene transcription. These results also imply that, similar to the effect of calcineurin inhibition, PARP-1 inhibition may be beneficial in modulating immune functions. ADP-ribosylation is a reversible posttranslational modification that transfers ADP-ribose from NAD to Glu, Asp, and/or Arg amino acids of target proteins (18). Similar to ubiquitination, ADP-ribosylation modifies target proteins to various masses due to the assorted chain lengths of the ADPribose. ADP-ribosylation is inhibited by the NAD analog 3-aminobenzamide and, more specifically, by PJ-34 (45). PolyADP-ribose polymerase-1 (PARP-1) is a nuclear enzyme that accounts for the bulk of ADP-ribosylation in vivo (43). Indeed, only 10% of PARP activity remains in Parp-1 / cells upon DNA damage. 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