Abstract
Gangliosides are important components of the membrane and are involved in many biological activities. St8sia5 is an α2,8-sialyltransferase involved in ganglioside synthesis, and has three isoforms. In this study, we analyzed the features of three isoforms, St8sia5-S, -M, and -L that had not been analyzed, and found that only St8sia5-L was localized in the Golgi, while the majority of St8sia5-M and -S were localized in the ER. The localization of Golgi of St8sia5 depended on the stem region. In addition, the incorporation of exogenous GD3 was upregulated only in St8sia5-L expressing cells. Taken together, the localization of St8sia5 is important for the activity of the enzyme.
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Acknowledgements
This research was supported in part by Grants-in-Aid for Scientific Research B (21H02425) and AMED (20ae0101069h0005) to CS and Grant-in-Aid for JSPS Fellows (EA). RH was supported by the Nagoya University CIBoG program from the MEXT WISE program.
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Araki, E., Hane, M., Hatanaka, R. et al. Analysis of biochemical features of ST8 α-N-acetyl-neuraminide α2,8-sialyltransferase (St8sia) 5 isoforms. Glycoconj J 39, 291–302 (2022). https://doi.org/10.1007/s10719-021-10034-8
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DOI: https://doi.org/10.1007/s10719-021-10034-8