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Updated: Sep 9, 2025

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
Published on: July 19, 2022
O-GlcNAcylation of CEP44 Promotes Its Droplet Formation and Regulates Its Localization
Mingzheng Hu1, Zihe Zhao1, Jinqiong Wang1
1Department of Genetics and Cell Biology, College of Life Sciences, State Key Laboratory of Medicinal Chemical Biology, Tianjin Union Medical Center, the First Affiliated Hospital of Nankai University, Nankai University, Tianjin, China.
Abstract:
The centrosomal protein of 44 kDa (CEP44) is essential for centriole duplication, centrosome cohesion, and spindle integrity. It localizes to the proximal end of centrioles and associates with spindle microtubules. Liquid-liquid phase separation (LLPS) is a process by which biomolecules undergo demixing into distinct liquid-like phases, facilitating the formation of cellular condensates such as the centrosome. However, whether CEP44 possesses LLPS properties remains unclear. In this study, we identified intrinsically disordered regions (IDRs) within CEP44, and droplet formation assays confirmed its capacity to form liquid droplets in vivo and in vitro. Immunoblotting detected O-GlcNAcylation of CEP44, indicating its interaction with O-GlcNAc transferase (OGT). Subsequent immunostaining demonstrated that O-GlcNAcylation promotes CEP44 droplet fusion. Post-translational modification prediction analysis suggested a potential interplay between O-GlcNAcylation and phosphorylation that may modulate the structural dynamics of CEP44. Overall, our findings reveal the LLPS capability of CEP44 and underscore the critical role of O-GlcNAcylation in regulating CEP44 droplet fusion and potentially influencing its subcellular localization.
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