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Cross-regulation of histone modifications

Nature Structural & Molecular Biology volume 14, pages 1017–1024 (2007)Cite this article

Abstract

Histones undergo several different post-translational modifications that control a variety of physiological processes. These covalent modifications show substantial cross-regulation, providing a wealth of regulatory potential. New insights into the communication between modifications on histones have emerged in recent years. This review assesses the current understanding of cross-regulation of histone modifications and identifies future questions to be addressed in this field.

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Figure 1: Histone modification choices.
Figure 2: Cross-regulation of modifications in cis and in trans.
Figure 3: Cross-talk between lysine methylation and lysine acetylation.
Figure 4: Potential for additional cross-regulation in nonhistone and histone proteins.

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Acknowledgements

We thank A. Loyola and R. Chosed for critical comments and suggestions. J.A.L. is supported in part by a fellowship by the American Legion Auxiliary. Aspects of this work were supported by US National Institutes of Health grant GM067718 and a grant from the Robert A. Welch Foundation (G1371) to S.Y.R.D. We apologize to colleagues whose work was not cited owing to space limitations.

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  1. Department of Biochemistry and Molecular Biology and Center for Epigenetics, Program in Genes and Development, University of Texas M. D. Anderson Cancer Center, Houston, 77030, Texas, USA

    John A Latham & Sharon Y R Dent

  2. Formerly known as Sharon Y. Roth.,

    Sharon Y R Dent

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Correspondence to Sharon Y R Dent.

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Latham, J., Dent, S. Cross-regulation of histone modifications. Nat Struct Mol Biol 14, 1017–1024 (2007). https://doi.org/10.1038/nsmb1307

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