Target intelligence / Profile preview

Solute carrier family 35 member B4 (SLC35B4)

Target
SLC35B4
Molecular classification
Transporter, Solute carrier family, Nucleotide sugar transporter
01

Overview

Solute carrier family 35 member B4 (SLC35B4) is a membrane transporter of the solute carrier family, specifically responsible for transporting the nucleotide sugars UDP-xylose and UDP-N-acetylglucosamine (UDP-GlcNAc) from the cytoplasm into the lumen of the endoplasmic reticulum and Golgi apparatus[1][2][5]. This transporter is essential for enabling glycosylation reactions catalyzed by glycosyltransferases, impacting the synthesis of glycoproteins, glycolipids, and proteoglycans[1][5]. SLC35B4 has been implicated in the regulation of cell proliferation and survival in cancers such as gastric carcinoma and hepatocellular carcinoma, where its overexpression correlates with poor prognosis[1][2]. Mechanistically, SLC35B4 promotes oncogenic processes by facilitating O-GlcNAcylation of key proteins (e.g., c-Myc) that stabilize them and drive tumorigenesis[2]. Human diseases associated with mutations or dysfunction of SLC35B4 include congenital disorder of glycosylation type IIC and Schneckenbecken dysplasia[5]. Therapeutically, it represents a plausible target, though no drugs directly targeting it are clinically available. Due to its central role in glycosylation, systemic inhibition poses considerable safety and developmental concerns[1][2][5].

Other names
Nucleotide sugar transporter SLC35B4YEA4PSEC0055FLJ14697UDP-xylose and UDP-N-acetylglucosamine transporterYEA4 homologUDP-Xylose/N-Acetylglucosamine transporter
02

Mechanism of action

Drugs targeting SLC35B4 would theoretically inhibit or alter nucleotide sugar transport, affecting glycosylation and potentially destabilizing oncogenic proteins like c-Myc via reduced O-GlcNAcylation

03

Biological functions

Transmembrane transport of nucleotide sugars (UDP-xylose, UDP-N-acetylglucosamine) from the cytoplasm to the endoplasmic reticulum and Golgi apparatusRegulation of protein glycosylation, glycolipid, and proteoglycan biosynthesisModulation of protein O-GlcNAcylationCellular proliferation and survival in cancer, especially in hepatic and gastric tissues
04

Disease associations

Cancer (notably hepatocellular carcinoma and gastric cancer)Congenital disorders of glycosylationSchneckenbecken dysplasia
05

Safety considerations

Disruption could broadly impact glycosylation of proteins and lipids, potentially causing metabolic or developmental defectsSince glycosylation is fundamental for normal cell function, targeting SLC35B4 systemically may risk toxicity and developmental abnormalities
06

Interacting drugs

None reported in current literature or major databases
07

Biomarkers

SLC35B4 expression level (prognostic biomarker in hepatocellular carcinoma and gastric cancer)O-GlcNAcylation state of proteins such as c-Myc

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