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Last update 08 May 2025

SLC35A1

Last update 08 May 2025

Basic Info

Synonyms

CMP-SA-Tr, CMP-Sia-Tr, CMP-sialic acid transporter

+ [6]

Introduction

Transports CMP-sialic acid from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges CMP-sialic acid for CMP (PubMed:12682060, PubMed:15576474, PubMed:23873973). Binds both CMP-sialic acid and free CMP, but has higher affinity for free CMP (By similarity). Also able to exchange CMP-sialic acid for AMP and UMP (PubMed:12682060). Also mediates the transport of CDP-ribitol (By similarity).

Drugs associated with SLC35A1

KI-8110

Target

SLC35A1

Mechanism

SLC35A1 inhibitors

Active Org.-

Originator Org.

Mect Corp.

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SLC35A1

100 Translational Medicine associated with SLC35A1

0 Patents (Medical) associated with SLC35A1

149

Literatures (Medical) associated with SLC35A1

01 Apr 2025·Journal of Biological Chemistry

CMP-sialic acid synthetase in Drosophila requires N-glycosylation of a non-canonical site

Article

Author: Monagas-Valentin, Pedro ; Scott, Hilary ; Panin, Vladislav ; Dauletbayeva, Saniya ; Mertsalov, Ilya ; Boland, Devon J ; Novikov, Boris

Sialylation plays important roles in animals, affecting numerous molecular and cell interactions. In Drosophila, sialylation regulates neural transmission and mediates communication between neurons and glia. Drosophila CMP-sialic acid synthetase (CSAS), a key enzyme of the sialylation pathway, is localized to the Golgi and modified by N-glycosylation, suggesting that this modification can affect CSAS function. Here we tested this hypothesis using in vitro and in vivo approaches. We found that CSAS proteins from divergent Drosophila species have two conserved N-glycosylation sites, including the rarely glycosylated non-canonical N-X-C sequon. We investigated CSAS glycosylation by generating CSAS "glycomutants" lacking glycosylation sites and analyzing them in vivo in transgenic rescue assays. The removal of non-canonical glycosylation significantly decreased CSAS activity, while the canonical site mutation did not affect CSAS function. Although all glycomutants were similarly localized to the Golgi, the non-canonical glycosylation, unlike the canonical one, affected CSAS stability in vivo and in vitro. Our results suggested that CSAS functions as a dimer, which was also supported by protein structure predictions that produced a dimer recapitulating the crystal structures of mammalian and bacterial counterparts, highlighting the evolutionary conservation of the CSAS structure-function relationship. This conclusion was supported by the rescue of CSAS mutants using the human ortholog. The non-canonical CSAS glycosylation was discussed in terms of a potential mechanism of temperature-dependent regulation of sialylation in poikilotherms that modulates neural activity in heat-shock conditions. Taken together, we uncovered an important regulation of sialylation in Drosophila, highlighting a novel interplay between glycosylation pathways in neural regulation.

01 Apr 2025·Journal of Biological Chemistry

Profiling the regulatory landscape of sialylation through miRNA targeting of CMP- sialic acid synthetase

Article

Author: Jame-Chenarboo, Faezeh ; Arachchige, Thusini Uggalla ; Mahal, Lara K ; Reyes, Joseph N

Cell surface sialic acid is an important glycan modification that contributes to both normal and pathological physiology. The enzyme cytidine monophosphate N-acetylneuraminic acid synthetase (CMAS) biosynthesizes the activated sugar donor cytidine monophosphate (CMP) sialic acid, which is required for all sialylation. CMAS levels impact sialylation with corresponding biological effects. The mechanisms that regulate CMAS are relatively uncharacterized. Herein, we use a high throughput genetically encoded fluorescence assay (miRFluR) to comprehensively profile the posttranscriptional regulation of CMAS by miRNA. These small non-coding RNAs have been found to impact glycosylation. Mapping the interactions of the human miRNAome with the 3'-untranslated region of CMAS, we identified miRNA whose impact on CMAS expression was either downregulatory or upregulatory. This follows previous work from our laboratory and others showing that miRNA regulation is bidirectional. Validation of the high-throughput results confirmed our findings. We also identified the direct binding sites for two upregulatory and two downregulatory miRNAs. Functional enrichment analysis for miRNAs upregulating CMAS revealed associations with pancreatic cancer, where sialic acid metabolism and the α-2,6-sialyltransferase ST6GAL1 have been found to be important. We found that miRNA associated with the enriched signature enhanced pancreatic cell-surface α-2,6-sialylation via CMAS expression in the absence of effects on ST6GAL1. We also find overlap between the miRNA regulation of CMAS and that of previously analyzed sialyltransferases. Overall, our work points to the importance of miRNA in regulating sialylation levels in disease and add further evidence to the bidirectional nature of miRNA regulation.

01 Apr 2025·International Journal of Biological Macromolecules

Corrigendum to “Genome-scale CRISPR screen identifies TRIM2 and SLC35A1 associated with porcine epidemic diarrhoea virus infection” [Int. J. Biol. Macromol. 250 (2023) 125962]

Author: Sun, Limeng ; Yin, Dongdong ; Wang, Jieru ; Liu, Hailong ; Zeng, Xiaoyu ; Yang, Yuqing ; Pan, Xiaocheng ; Zhao, Shuhong ; Li, Sheng ; Peng, Guiqing ; Tan, Yubei ; Ruan, Jinxue ; Wang, Chonglong ; Xie, Shengsong ; Wang, Zichang ; Shen, Xuehuai ; Yin, Lei ; Li, Xinyun ; Dai, Yin ; Guo, Zishi ; Liu, Xiangdong

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SLC35A1

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