O-GlcNAcylation regulates phagocytosis by promoting Ezrin localization at the cell cortex.

Song Yang, Hanyu Liu, Hua Ni, Lingyu Jiang, Mulin Yang, Quan Chen, Jun Zhou, Fan Yu

Journal of genetics and genomics = Yi chuan xue bao 2023 Jul

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O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes. However, it remains uncertain whether O-GlcNAcylation is involved in the regulation of phagocytosis. Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli. Knockout of the O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function. Mechanistic studies reveal that the O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation. Our data further show that Ezrin O-GlcNAcylation promotes its localization to the cell cortex, thereby stimulating the membrane-cytoskeleton interaction needed for efficient phagocytosis. These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases. Copyright © 2023 Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, and Genetics Society of China. Published by Elsevier Ltd. All rights reserved.

Citation

Song Yang, Hanyu Liu, Hua Ni, Lingyu Jiang, Mulin Yang, Quan Chen, Jun Zhou, Fan Yu. O-GlcNAcylation regulates phagocytosis by promoting Ezrin localization at the cell cortex. Journal of genetics and genomics = Yi chuan xue bao. 2023 Jul;50(7):486-496