Due to a production error, there was a mistake in the published legend of Figure 4, resulting in the incorrect use and duplication of the legend for Figure 3. The corrected Figure 4 and its legend appear below.
Figure 4
Glycosylation patterns of the KCC2-CTD mutants. (A) Top panel: Western blot analysis of KCC2 polypeptides in the total protein lysates of HEK293 cells expressing KCC2-CTD mutants, using a KCC2 antibody recognizing the C-terminal epitope. Two bands around 130-kDa corresponding to the putative glycosylated forms of monomeric KCC2 are observed. Bottom panel: To ensure equal amounts of total proteins loaded on SDS–PAGE, blots were analyzed with the antibody recognizing α-Tubulin. (B) PNGase F treatment removes all N-linked oligosaccharides from the KCC2 polypeptides, thus shifting the KCC2 bands to their predicted unglycosylated molecular weight of 123.6-kDa. (C) Endo H treatment shifts down the 125-kDa band corresponding to the A7, A8, and B1 KCC2 mutants, which contain mainly ER-added high-mannose glycans but leaves intact the 140-kDa KCC2 band corresponding to the B8 and C1 mutants, which contain mainly Golgi-added complex glycans.
The publisher apologizes for this mistake.
The original article has been updated.
Summary
Keywords
KCC2, SLC12A5, GABA, chloride homeostasis, Mu transposon mutagenesis, KCC2-CTD mutations
Citation
Frontiers Production Office (2025) Erratum: Uncovering novel KCC2 regulatory motifs through a comprehensive transposon-based mutant library. Front. Mol. Neurosci. 18:1576660. doi: 10.3389/fnmol.2025.1576660
Received
14 February 2025
Accepted
14 February 2025
Published
25 February 2025
Approved by
Frontiers Editorial Office, Frontiers Media SA, Switzerland
Volume
18 - 2025
Updates
Copyright
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