Abstract
CMP-sialic acid is a donor substrate of sialyltransferases. CMP-sialic acid transporter (CST) couples with the antiport of CMP and transports CMP-sialic acid from the cytosol into the lumen of the medial and trans cisternae of the Golgi apparatus, where sialylation is mediated by a variety of sialyltransferases. Therefore, expression of CST regulates the sialylation of glycans on the cell surface. CST is categorized as the first member of subgroup A of Solute carrier family 35 (SLC35A1). CST activity was initially identified in microsomal membrane vesicles prepared from mouse liver. To date, CST genes from the mouse, human and two plant species have been expressed in a yeast expression system and their CST activities proved by an in vitro CMP-sialic acid transport assay using yeast Golgi enriched vesicles. In humans, inactivation of both CST alleles has been found to cause congenital glycosylation type IIf disorder in which the affected patient showed macrothrombocytopenia and neutropenia.
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Nishihara, S. (2014). Solute Carrier Family 35 (CMP-Sialic Acid Transporter), Member A1 (SLC35A1). In: Taniguchi, N., Honke, K., Fukuda, M., Narimatsu, H., Yamaguchi, Y., Angata, T. (eds) Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54240-7_98
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DOI: https://doi.org/10.1007/978-4-431-54240-7_98
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