Covalent modifications of RUNX proteins: Structure affects function

Ezra Blumenthal, Sarah Greenblatt, Guang Huang, Koji Ando, Ye Xu, Stephen D Nimer

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

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.

Original languageEnglish (US)
Title of host publicationAdvances in Experimental Medicine and Biology
PublisherSpringer New York LLC
Pages33-44
Number of pages12
Volume962
DOIs
StatePublished - 2017

Publication series

NameAdvances in Experimental Medicine and Biology
Volume962
ISSN (Print)00652598
ISSN (Electronic)22148019

Keywords

  • Acetylation
  • Acute myeloid leukemia
  • CBFβ
  • Cleidocranial dysplasia
  • FPD/AML
  • Methylation
  • Phosphorylation
  • Post-translational modifications
  • RUNX1
  • RUNX2
  • RUNX3
  • Transcriptional activation
  • Transcriptional repression
  • Ubiquitylation

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Blumenthal, E., Greenblatt, S., Huang, G., Ando, K., Xu, Y., & Nimer, S. D. (2017). Covalent modifications of RUNX proteins: Structure affects function. In Advances in Experimental Medicine and Biology (Vol. 962, pp. 33-44). (Advances in Experimental Medicine and Biology; Vol. 962). Springer New York LLC. https://doi.org/10.1007/978-981-10-3233-2_3