Abstract
The RUNX family of transcription factors plays important roles in tissue-specific gene expression. Many of their functions depend on specific post-translational modifications (PTMs), and in this review, we describe how PTMs govern RUNX DNA binding, transcriptional activity, protein stability, cellular localization, and protein-protein interactions. We also report how these processes can be disrupted in disease settings. Finally, we describe how alterations of RUNX1, or the enzymes that catalyze its post-translational modifications, contribute to hematopoietic malignancies.
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We are grateful to Delphine Prou, Ph.D., for her helpful suggestions and comments.
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Blumenthal, E., Greenblatt, S., Huang, G., Ando, K., Xu, Y., Nimer, S.D. (2017). Covalent Modifications of RUNX Proteins: Structure Affects Function. In: Groner, Y., Ito, Y., Liu, P., Neil, J., Speck, N., van Wijnen, A. (eds) RUNX Proteins in Development and Cancer. Advances in Experimental Medicine and Biology, vol 962. Springer, Singapore. https://doi.org/10.1007/978-981-10-3233-2_3
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DOI: https://doi.org/10.1007/978-981-10-3233-2_3
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