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Updated: Jan 20, 2026

Phloem and Sugar Transport in Plants

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Nucleotide Sugar Transporter SLC35 Family Structure and Function.

Barbara Hadley¹, Thomas Litfin², Chris J Day¹

¹Institute for Glycomics, Griffith University, Gold Coast Campus, Queensland 4222, Australia.

Computational and Structural Biotechnology Journal

|August 30, 2019

Summary

Nucleotide sugar transporters (NSTs) are crucial for glycosylation. Recent advances clarify the function of poorly understood NSTs (SLC35 family) and reveal the first crystal structures, enabling new models for sugar transport.

Keywords:

CMP-sialic acid transporter Endoplasmic reticulum Golgi apparatus Nucleotide sugar transporters SLC35

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Phloem and Sugar Transport in Plants

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Orthologous & Homologous Genes and Gene Families

Orthologous & Homologous Genes and Gene Families

Protein Families and Superfamilies & Classification Database

Protein Families and Superfamilies & Classification Database

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Glycosylation is vital for cellular processes, relying on nucleotide sugar transporters (NSTs) to move activated sugars.
The SLC35 family of solute transporters plays a critical role in connecting sugar synthesis to glycosylation machinery in the ER and Golgi.

Purpose of the Study:

To provide a comprehensive update on recent advancements in the field of nucleotide sugar transporters (NSTs).
To highlight progress in understanding the function and substrate specificity of various SLC35 family members.
To present new structural insights and mechanistic models for NSTs, including the CMP-sialic acid transporter (CST).

Main Methods:

Review of recent literature on SLC35 family transporters.
Analysis of functional data and substrate specificity studies for key NSTs.
Structural biology approaches, including crystal structure determination and homology modeling.
In silico modeling and analysis of transporter mechanisms and mutations.

Main Results:

Significant progress has been made in elucidating the function of previously poorly understood NSTs like SLC35 A4, A5, and D3.
Insights into the regulation of SLC35A2 and SLC35A3 association and the impact of mutations on SLC35B4 localization.
The first crystal structure of a yeast NST homolog (Vrg-4) has been determined, facilitating new models for human NSTs like CST (SLC35A1).
Models for CST function, including isoform-specific activity and potential monomer/dimer mechanisms, have been proposed.
Updates on two additional NST crystal structures are provided.

Conclusions:

Recent structural and functional studies have significantly advanced our understanding of NSTs within the SLC35 family.
New models provide mechanistic insights into sugar transport and regulation, with implications for various cellular processes.
The availability of crystal structures is paving the way for deeper mechanistic investigations and potential therapeutic targeting.