Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P51532 (
transcriptional activator
)
6,546
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
TonEBP [TonE (tonicity-responsive enhancer)-binding protein] is a
transcriptional activator
of the Rel family like NF-kappaB (nuclear factor kappaB) and NFAT (nuclear factor of activated T-cells). TonEBP plays a key role in the protection of cells in the kidney medulla from the deleterious effects of hyperosmolality. This is achieved by enhancing expression of HSP70 (heat-shock protein 70) and other genes whose products drive cellular accumulation of organic osmolytes. TonEBP is stimulated by ambient hypertonicity via multiple pathways that regulate nuclear translocation and transactivation. In the present paper, we report that TonEBP is associated in vivo with RHA (
RNA helicase A
). The N- and C-termini of RHA bound the E'F loop of the DNA-binding domain of TonEBP. The interaction was not affected by DNA binding or dimerization of TonEBP. Overexpression of RHA inhibited the activity of TonEBP; however, catalytic activity of RHA was dispensable for the inhibition. When the ambient tonicity was raised, the TonEBP-RHA interaction decreased, suggesting that dissociation of RHA is a pathway to stimulate TonEBP. We conclude that the E'F loop of TonEBP interacts with RHA like NFAT and NF-kappaB interact with AP1 (activator protein 1) and the high-mobility group protein HMG-I(Y) respectively. While RHA interacts with and stimulates other transcription factors such as CREB (cAMP-response-element-binding protein), NF-kappaB and mineralocorticoid receptor, it inhibits TonEBP.
...
PMID:TonEBP is inhibited by RNA helicase A via interaction involving the E'F loop. 1617 19
Zic2 is a
transcriptional activator
that plays a crucial role in mammalian forebrain development. It activates the transcription of target genes by DNA binding and recruitment of
RNA helicase A
(
RHA
). We recently reported that the Zic2-
RHA
interaction is decreased by phosphatase treatment in vitro. We have now identified the phosphorylation site (serine 200) in mouse Zic2. Zic2S200A was defective in
RHA
-binding, and its transcriptional activation ability was diminished. These data indicate that Zic2S200 is a target for phosphorylation by DNA-dependent protein kinase, regulating Zic2-mediated transcriptional activation.
...
PMID:Functional role of Zic2 phosphorylation in transcriptional regulation. 1806 28
