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Phanor, S. K.

Publications and source records attributed to Phanor, S. K..

2 recordsLinked to original sources

NKX2-5 congenital heart disease mutations show diverse loss and gain of epigenomic, biochemical and chromatin search functions underpinning pathogenicity

Congenital heart defects (CHD) occur in [~]1% of live births, with inherited and acquired mutations and environmental factors contributing to causation. However, network perturbations in CHD remain poorly understood. We report an integrated functional-epigenomics approach to CHD, focusing on the cardiac homeodomain (HD) transcription factor NKX2-5, mutations which cause diverse heart structural and conduction defects. We selected twelve NKX2-5 CHD variants affecting different residue classes - homeodomain DNA base-contacting, backbone-contacting and helix-stabilizing, and those affecting other conserved protein:protein interaction (PPI) domains. In HL-1 cardiomyocytes, we profiled genome-wide DNA targets of NKX2-5 wild type (WT) and variants, their DNA binding affinity and specificity, PPI with known NKX2-5 cofactors and chromatin search dynamics. Variants showed diverse yet class-specific behaviours. All variants failed to bind many WT targets but retained binding to a subset of core cardiomyocyte-related targets, and bound hundreds of unique "off-targets" via changes to DNA binding site specificity, homodimerization, cofactor interactions and chromatin search functions. Our data suggest that complex residue-by-residue scale epigenomic, biochemical and chromatin search defects involving both loss-and gain-of-function contribute to CHD. These findings may inform precision molecular therapeutic approaches in patients with CHD.

genomics↗

DNA binding analysis of rare variants in homeodomains reveals novel homeodomain specificity-determining residues

Homeodomains (HDs) are the second largest class of DNA binding domains (DBDs) among eukaryotic sequence-specific transcription factors (TFs) and play important roles in regulating development, body patterning, and cellular differentiation. Here, we analyzed 92 human HD mutants, including disease-associated variants and variants of unknown significance (VUSs), for their effects on DNA binding activity. Many of the variants altered DNA binding affinity and/or specificity. Biochemical analysis and structural modeling identified 14 novel specificity-determining positions, 5 of which do not contact DNA. The same missense substitution at analogous positions within different HDs often exhibited different effects on DNA binding. Variant effect prediction tools perform moderately well in distinguishing variants with altered binding affinity, but poorly in identifying those with altered specificity. Our results highlight the need for biochemical assays of TF coding variants and prioritize dozens of variants for further investigations into their pathogenicity and development of clinical diagnostics and precision therapies.

genetics↗