Covalent Modifications of RUNX Proteins: Structure Affects Function
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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PTMs can alter the DNA binding activity and cofactor interactions of transcription factors.
“These modifications can alter the DNA binding activity and cofactor interactions of TFs, representing highly tractable targets for modulation of TF activity.643,644”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [644]
A 2014 proteomics study identified 222 PTMs of 99 residues on p53, a tumor suppressor protein.
“In 2014, a proteomics study identified 222 PTMs of 99 residues on p53, a tumor suppressor protein.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [644]
PTMs of transcription factors represent highly tractable targets for modulation of TF activity.
“These modifications can alter the DNA binding activity and cofactor interactions of TFs, representing highly tractable targets for modulation of TF activity.643,644”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [644]
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- Authors
- Blumenthal, E., Greenblatt, S., Huang, G., Ando, K., Xu, Y., & Nimer, S. D.
- Affiliations
- Sylvester Comprehensive Cancer Center (US)
- Cincinnati Children's Hospital Medical Center (US)
- University of Miami (US)
- Corresponding author
- Nimer, Stephen D.
- Venue
- Advances in Experimental Medicine and Biology
- Publisher
- Springer Singapore
- Published
- 2017
- Volume
- 962
- Pages
- 33-44
- ISSN
- 0065-2598 (ISSN-L)
- 2214-8019
- OpenAlex
- W2613674886
- Cited by
- 16
- References
- 68
- Citations by year
- 2023: 1 · 2022: 1 · 2021: 4 · 2020: 4 · 2019: 2 · 2018: 3 · 2017: 1
- FWCI
- 3.40
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Advances in experimental medicine and biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Keywords
- post-translational modification, RUNX1, transcription factors, DNA binding, transcriptional activity, protein stability, protein-protein interaction, subcellular localization, hematologic malignancies, epigenetic regulation
- MeSH terms
- Animals, DNA-Binding Proteins, Humans, Protein Processing, Post-Translational, Transcription Factors, Transcription, Genetic, Core Binding Factor alpha Subunits, Protein Interaction Maps
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