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. 2024 Mar 5;16(5):1048. doi: 10.3390/cancers16051048

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© 2024 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Elevated levels of mOGT reduce phosphorylation of respiratory chain proteins and mediate their O-GlcNAcylation. (A) O-GlcNAcylation levels of ETM components determined by Western blot; (B) p-Ser/p-Thr expression of isolated ETM proteins determined by Western blot; (C) Venn diagram showing the total number of identified ETM mOGT candidates common with ETM components according to the MitoCart 3.0 datasets (Broad Institute) and O-GlcNAcylated proteins according to the Human O-GlcNAcome Database ver. 1.3 (Medical College of Wisconsin); (D) The graph presents identified ETM mOGT candidates in three analyzed cell lines; (E) Venn diagram showing mOGT candidates common to all analyzed cell lines previously identified as ETM O-GlcNAcylated proteins according to the MitoCart 3.0 datasets and the Human O-GlcNAcome Database ver. 1.3.