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

Open access
Perlmann, T, Jansson, L·1995·Genes & Development

Abstract

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.

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Metadata

Authors
Perlmann, T., & Jansson, L.
Venue
Genes & Development
Published
1995-04-01
Volume
9
Issue
7
Pages
769-782
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2111897372
Cited by
546
References
3
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1. https://app.cochat.ai/papers/10.1101/gad.9.7.769
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Perlmann, T., & Jansson, L. (1995). A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1. Genes & Development. https://doi.org/10.1101/gad.9.7.769

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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