A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1.

• T Perlmann

• L Jansson

抄録

In addition to its role as a 9-cis retinoic acid receptor, RXR has an important role in the regulation of multiple hormonal pathways through heterodimerization with nuclear receptors. Here, we show that two orphan receptors, NGFI-B and NURR1, which have been shown previously to interact with DNA as monomers, also can heterodimerize with RXR. These heterodimers bind selectively to a class of retinoic acid response elements composed of direct repeats spaced by 5 nucleotides. In this respect they are similar to heterodimers formed between RXR and the receptor for all-trans retinoic acid, RAR. However, whereas RXR is inhibited in the RXR-RAR heterodimer, NGFI-B/NURR1 promote efficient activation in response to RXR ligands and therefore shift RXR from a silent to an active heterodimerization partner. These data show that NGFI-B and NURR1 can increase the potential of RXR to modulate gene expression in a ligand-dependent manner by allowing a distinct class of direct repeats to serve as specific RXR response elements. Because expression of both NGFI-B and NURR1 is rapidly induced by various growth factors, these findings also suggest a novel mechanism for convergence between vitamin A or retinoid and growth factor signaling pathways.

収録刊行物

• Genes & Development

  Genes & Development 9 (7), 769-782, 1995-04-01

  Cold Spring Harbor Laboratory

キーワード

• Developmental Biology
• Genetics

詳細情報

• CRID: 1363107371184395520
• NII論文ID: 80008251340
• DOI: 10.1101/gad.9.7.769
• ISSN: 15495477
• ISSN: 08909369
• ISSN: http://id.crossref.org/issn/08909369
• Web Site: https://syndication.highwire.org/content/doi/10.1101/gad.9.7.769
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