Covalent Modifications of RUNX Proteins: Structure Affects Function.
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.
['Blumenthal|Ezra|E|', 'Greenblatt|Sarah|S|', 'Huang|Guang|G|', 'Ando|Koji|K|', 'Xu|Ye|Y|', 'Nimer|Stephen D|SD|']
D000818:Animals D050657:Core Binding Factor alpha Subunits D004268:DNA-Binding Proteins D006801:Humans D060066:Protein Interaction Maps D011499:Protein Processing, Post-Translational D014157:Transcription Factors D014158:Transcription, Genetic
Post-Translational Modifications Transcriptional Activation RUNX1 Acetylation Acute Myeloid Leukemia CBFβ Cleidocranial Dysplasia FPD/AML Methylation Phosphorylation RUNX2 RUNX3 Transcriptional Repression Ubiquitylation