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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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Dimerization is required for phosphorylation and DNA binding of TonEBP/NFAT5

Cited 30 times inthomson ciCited 23 times inthomson ci
Title
Dimerization is required for phosphorylation and DNA binding of TonEBP/NFAT5
Author
Lee, SDWoo, SKKwon, H. Moo
Keywords
rel-homology domain; hypertonicity; hypotonicity
Issue Date
200206
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.294, no.5, pp.968 - 975
Abstract
TonEBP (NFAT5) is a newly identified member of the Rel family of transcriptional activators that include NF-kappaB and NFAT1 to NFAT4. Activated in response to hypertonicity, TonEBP stimulates transcription of transporters of organic osmolytes, certain cytokines, and a molecular chaperone. We provide biochemical data demonstrating that full-length TonEBP dimerizes via the C-terminus of the Rel-homology domain (CRHD). The two polyglutamine motifs were not involved. The dimerization was not affected by nucleocytoplasmic shifts in TonEBP in response to changes in ambient tonicity. Preventing the dimer formation by deleting the CRHD did not affect the nucleocytoplasmic shifts. On the other hand, deletion of the CRHD prevented DNA binding and eliminated the dominant negative activity of a C-terminal truncated TonEBP. Furthermore, phosphorylation was dramatically reduced especially in hypertonic conditions by deletion of the CRHD. We conclude that dimerization is required for proper phosphorylation of TonEBP as well as DNA binding.
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DOI
http://dx.doi.org/10.1016/S0006-291X(02)00572-7
ISSN
0006-291X
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