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CORRECTION article

Front. Neurosci., 22 September 2025

Sec. Neurodevelopment

Volume 19 - 2025 | https://doi.org/10.3389/fnins.2025.1694725

Correction: Role of the YWHAG gene mutations in developmental and epileptic encephalopathy

  • Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL, United States

A Correction on
Role of the YWHAG gene mutations in developmental and epileptic encephalopathy

by Vilmont, V., Nowakowski, R. S., and Zhou, Y. (2025). Front. Neurosci. 19:1641250. doi: 10.3389/fnins.2025.1641250

There was a mistake in the caption of Figure 6 as published. There was a mistake at the end of the Figure 6 legend, stating the source of the Figure 6. The statement “Source: Logue et al. (2024)” is incorrect, and must be replaced with “Created in Biorender”. The corrected caption of Figure 6 appears below.

There was a mistake in the caption of Figure 7 as published. There was a mistake at the end of the Figure 7 legend, stating how Figure 7 was created. The statement “Created in Biorender” is incorrect, and must be removed. Figure 7 was not created in Biorender, it was a reference figure taken from Logue et al. (2024). The corrected caption of Figure 7 appears below.

The figures 1 and 2 were in the wrong order, and the figures 6 and 7 were in the wrong order. The images of Figure 1 and Figure 2 are incorrect and must be switched with each other; the figure captions and legends are correct as published. The images of Figures 6 and 7 are incorrect and must be switched with each other. The figure order has now been corrected.

Figure 1
Protein interaction network diagram showing connections between proteins YAP1, RAF1, BRAF, ARAF, CDC25C, CDC25B, HDAC4, and several YWHA proteins. Lines indicate interactions: pink for experimentally determined, blue for curated databases, green for gene neighborhood, red for gene fusions, black for gene co-occurrence, yellow for text mining, turquoise for co-expression, and purple for protein homology.

Figure 1. Functional interaction network of 14-3-3γ encoded by YWHAG. Network nodes are labeled with the name of the individual genes which encode the represented proteins. Protein interactions are represented by color coded lines, based on known and predicted interactions, as indicated by the legend. Source: https://stringdb.org/cgi/network?taskId=bMYGzw1kOtuv&sessionId=bMliKFIeKj5g. Screenshot image obtained from the STRING database (string-db.org). Licensed under the Creative Commons Attribution 4.0 International License (CC BY 4.0).

Figure 2
Bar graph showing nTPM values for various tissues. The cerebral cortex has the highest value, followed by adipose tissues, small intestine, and stomach. Other tissues have significantly lower values. Color-coded bars represent different tissues.

Figure 2. RNA tissue specificity expression of 14-3-3γ. Normalized RNA expression levels (nTPM) shown for 55 tissue types. Color coding is based on tissue groups, each consisting of tissues with functional features in common. RNA tissue specificity expression is enhanced in brain (yellow bars) and skeletal muscle cells (brown bars). Source: https://www.proteinatlas.org/ENSG00000170027-YWHAG/tissue. Screenshot image obtained from the Human Protein Atlas (proteinatlas.org). Licensed under the Creative Commons Attribution-ShareAlike 4.0 International License (CC BY-SA 4.0).

Figure 6
Diagram illustrating the effects of mutations on YWHAG. Panel A shows wildtype YWHAG with functional dimers binding ligands. Panel B shows heterozygous truncating mutation causing non-functional, shorter subunits unable to dimerize. Panel C displays heterozygous missense mutation with three scenarios of non-functional dimers unable to bind ligands.

Figure 6. Impact of heterozygous truncating and missense YWHAG mutations on 14-3-3γ dimer formation and function. (A) The wildtype YWHAG gene produces normal 14-3-3γ subunits, which assemble into functional 14-3-3γ dimers, able to bind phosphorylated ligands. (B) A truncating mutation produces non-functional mutant 14-3-3γ subunits that are shorter and smaller, which are unable to dimerize and to bind phosphorylated ligands. (C) A missense mutation produces non-functional mutant 14-3-3γ subunits that are the same size as the wildtype subunits, which are able to dimerize but unable to bind two phosphorylated ligands. WT, wildtype; MT, mutant. Created in Biorender.

Figure 7
Panel A shows two microscopy images comparing 14-3-3 FKO and wild type with visible differences. Panel B presents electroencephalogram traces indicating neuronal activity in both conditions, showing increased activity in 14-3-3 FKO, even after synaptic blockers. Panel C is a bar graph comparing frequency (Hz) before and after blockers, with higher values in 14-3-3 FKO. Significant differences are indicated by asterisks.

Figure 7. 14-3-3 FKO hippocampal CA1 neurons fire more APs than WT neurons in the presence and absence of synaptic blockers. (A) Hippocampal slice images captured using phase contrast and fluorescence microscopy show 14-3-3 FKO neurons (left) identified by their YFP fluorescence, indicating difopein expression. (B) Traces of spontaneous AP firing in 14-3-3 FKO and WT neurons under whole-cell configuration, before and after synaptic blocker application. (C) Group data showing a higher AP firing rate for 14-3-3 FKO cells (n = 9 before blockers, 6 after blockers) than WT cells (n = 9 before blockers, 8 after blockers). AP, action potential; FKO, functional knockout; WT, wildtype; CA1, one of four hippocampal subfields that make up hippocampus structure. Source: Figure 1 from Logue et al. (2024).

The original version of this article has been updated.

Keywords: YWHAG mutation, 14-3-3γ protein, developmental and epileptic encephalopathy, epilepsy, seizure, neuronal hyperexcitability, DEE, 14-3-3 protein family

Citation: Vilmont V, Nowakowski RS and Zhou Y (2025) Correction: Role of the YWHAG gene mutations in developmental and epileptic encephalopathy. Front. Neurosci. 19:1694725. doi: 10.3389/fnins.2025.1694725

Received: 28 August 2025; Accepted: 29 August 2025;
Published: 22 September 2025.

Approved by:

Frontiers Editorial Office, Frontiers Media SA, Switzerland

Copyright © 2025 Vilmont, Nowakowski and Zhou. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Yi Zhou, WWkuWmhvdUBtZWQuZnN1LmVkdQ==

ORCID: Violet Vilmont orcid.org/0009-0001-9410-6628

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