{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,29]],"date-time":"2026-03-29T13:17:55Z","timestamp":1774790275802,"version":"3.50.1"},"reference-count":36,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,1,1]]},"abstract":"<jats:p>TonEBP [TonE (tonicity-responsive enhancer)-binding protein] is a transcriptional activator of the Rel family like NF-\u03baB (nuclear factor \u03baB) 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\u2032F 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\u2013RHA interaction decreased, suggesting that dissociation of RHA is a pathway to stimulate TonEBP. We conclude that the E\u2032F loop of TonEBP interacts with RHA like NFAT and NF-\u03baB 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-\u03baB and mineralocorticoid receptor, it inhibits TonEBP.<\/jats:p>","DOI":"10.1042\/bj20051082","type":"journal-article","created":{"date-parts":[[2005,12,14]],"date-time":"2005-12-14T13:01:28Z","timestamp":1134565288000},"page":"411-419","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["TonEBP is inhibited by RNA helicase A via interaction involving the E\u2032F loop"],"prefix":"10.1042","volume":"393","author":[{"given":"Emanuela","family":"Colla","sequence":"first","affiliation":[{"name":"Department of Medicine, University of Maryland, 22 South Greene Street, Suite N3W143, Baltimore, MD 21201, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sang\u00a0D.","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Maryland, 22 South Greene Street, Suite N3W143, Baltimore, MD 21201, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mee\u00a0R.","family":"Sheen","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Maryland, 22 South Greene Street, Suite N3W143, Baltimore, MD 21201, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Seung\u00a0K.","family":"Woo","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Maryland, 22 South Greene Street, Suite N3W143, Baltimore, MD 21201, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.\u00a0Moo","family":"Kwon","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Maryland, 22 South Greene Street, Suite N3W143, Baltimore, MD 21201, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2005,12,12]]},"reference":[{"key":"2021112213433394100_B1","doi-asserted-by":"crossref","first-page":"2538","DOI":"10.1073\/pnas.96.5.2538","article-title":"Tonicity-responsive enhancer binding protein, a Rel-like protein that stimulates transcription in response to hypertonicity","volume":"96","author":"Miyakawa","year":"1999","journal-title":"Proc. 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