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Cited by 588

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Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3- 3-dependent cellular localization

Open access
Grozinger, Christina M., Schreiber, Stuart L.·2000·Proceedings of the National Academy of Sciences

Abstract

Transcription is controlled in part by the dynamic acetylation and deacetylation of histone proteins. The latter process is mediated by histone deacetylases (HDACs). Previous analysis of the regulation of HDAC activity in transcription has focused primarily on the recruitment of HDAC proteins to specific promoters or chromosomal domains by association with DNA-binding proteins. To characterize the cellular function of the recently identified HDAC4 and HDAC5 proteins, complexes were isolated by immunoprecipitation. Both HDACs were found to interact with14-3-3 proteins at three phosphorylation sites. The association of 14-3-3 with HDAC4 and HDAC5 results in the sequestration of these proteins in the cytoplasm. Loss of this interaction allows HDAC4 and HDAC5 to translocate to the nucleus, interact with HDAC3, and repress gene expression. Regulation of the cellular localization of HDAC4 and HDAC5 by 14-3-3 represents a mechanism for controlling the transcriptional activity of these class II HDAC proteins.

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Metadata

Authors
Grozinger, C. M., & Schreiber, S. L.
Venue
Proceedings of the National Academy of Sciences
Published
2000-06-27
Volume
97
Issue
14
Pages
7835-7840
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2133446638
Cited by
588
References
5
FWCI
12.17
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3- 3-dependent cellular localization. https://app.cochat.ai/papers/10.1073/pnas.140199597
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Grozinger, C. M., & Schreiber, S. L. (2000). Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3- 3-dependent cellular localization. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.140199597

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.