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Author

Kwon, H. Moo
Inflammation and Kidney Disorder Lab
Research Interests
  • TonEBP, Obesity, Cancer, Chronic inflammatory diseases, Brain disorder, Kidney disorders, Genomic instability

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Multiple domains of TonEBP cooperate to stimulate transcription in response to hypertonicity

Cited 1 times inthomson ciCited 36 times inthomson ci
Title
Multiple domains of TonEBP cooperate to stimulate transcription in response to hypertonicity
Author
Do Lee, SColla, ESheen, MRNa, KYKwon, H. Moo
Keywords
ENHANCER-BINDING PROTEIN; NF-KAPPA-B; GENE-TRANSCRIPTION; DNA-BINDING; TONICITY; ACTIVATION; CELLS; PHOSPHORYLATION; DROSOPHILA; SCREEN
Issue Date
200311
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.48, pp.47571 - 47577
Abstract
Tonicity-responsive enhancer binding protein (TonEBP), also known as NFAT5, belongs to the Rel family of transcriptional activators. In the kidney medulla and thymus, TonEBP plays a major role in protecting renal cells and T cells from the deleterious effects of ambient hypertonicity. TonEBP is stimulated by hypertonicity via several pathways: increased expression of protein, nuclear translocation, and increased transactivation. In this study, we identified five domains of TonEBP involved in transactivation. The two conserved glutamine repeats were not involved in transactivation. There were three activation domains that could stimulate transcription independently. In addition, there were two modulation domains that potentiated the activity of the activation domains. One of the activation domains is unique to a splice isoform that is more active than others, indicating that alternative splicing can affect the activity of TonEBP. Another activation domain and one of the modulation domains were stimulated by hypertonicity. All the five domains acted in synergy in every combination. Although overall phosphorylation of TonEBP increased in response to hypertonicity, phosphorylation of the activation and modulation domains did not increase in isolation. In sum, TonEBP possesses far more elaborate domains involved in transactivation compared with other Rel proteins.
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DOI
http://dx.doi.org/10.1074/jbc.M308795200
ISSN
0021-9258
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