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Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity.

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Hai, T, Curran, T·1991·Proceedings of the National Academy of Sciences

Abstract

The Fos/Jun and ATF/CREB families of transcription factors function in coupling extracellular signals to alterations in expression of specific target genes. Like many eukaryotic transcription factors, these proteins bind to DNA as dimers. Dimerization is mediated by a structure known as the "leucine-zipper" motif. Although Fos/Jun and ATF/CREB were previously thought to interact preferentially with different DNA regulatory elements (the AP-1/TRE and ATF/CRE sites, respectively), we find that members of these two families form selective cross-family heterodimers. The resulting heterodimers display distinguishable DNA binding specificities from each other and from their parental homodimers. These findings indicate that the Fos/Jun and ATF/CREB families of transcription factors are not as distinct as was previously thought. We suggest that they can be grouped into a superfamily of transcription factors.

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Metadata

Authors
Hai, T., & Curran, T.
Venue
Proceedings of the National Academy of Sciences
Published
1991-05
Volume
88
Issue
9
Pages
3720-3724
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2023666553
Cited by
1,294
References
1
FWCI
23.21
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. https://app.cochat.ai/papers/10.1073/pnas.88.9.3720
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Hai, T., & Curran, T. (1991). Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.9.3720

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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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