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Updated: Apr 3, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Glycosylation of solute carriers: mechanisms and functional consequences
Nis Borbye Pedersen1, Michael C Carlsson2, Stine Falsig Pedersen3
1Section of Cell Biology and Physiology, Department of Biology, Faculty of Science, University of Copenhagen, Copenhagen O, Denmark. nis.pedersen@bio.ku.dk.
Abstract:
Solute carriers (SLCs) are one of the largest groups of multi-spanning membrane proteins in mammals and include ubiquitously expressed proteins as well as proteins with highly restricted tissue expression. A vast number of studies have addressed the function and organization of SLCs as well as their posttranslational regulation, but only relatively little is known about the role of SLC glycosylation. Glycosylation is one of the most abundant posttranslational modifications of animal proteins and through recent advances in our understanding of protein-glycan interactions, the functional roles of SLC glycosylation are slowly emerging. The purpose of this review is to provide a concise overview of the aspects of glycobiology most relevant to SLCs, to discuss the roles of glycosylation in the regulation and function of SLCs, and to outline the major open questions in this field, which can now be addressed given major technical advances in this and related fields of study in recent years.
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