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PubMed · 17116477

Regulating cell surface glycosylation with a small-molecule switch.

Danielle H Dube·Christopher L de Graffenried·Jennifer J Kohler
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Abstract

Correct localization of Golgi-resident enzymes is essential for the formation of specific glycan epitopes. In this chapter, we describe a method to control the localization, and thus the activity, of an individual glycosyltransferase by administration of a small molecule. Our method takes advantage of the modularity of most Golgi-resident enzymes, which are composed of localization and catalytic domains. These domains can be physically separated and fused to the small molecule binding proteins FRB and FKBP, which dimerize in the presence of rapamycin. In this way, rapamycin serves as a "switch" for enzyme activity.

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Catalytic DomainEpitopesGlycosylationGlycosyltransferasesGolgi ApparatusHumansImmunosuppressive AgentsMembrane ProteinsModels, MolecularPolysaccharidesProtein Structure, TertiarySirolimusTacrolimus Binding ProteinsJournal Article

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Danielle H Dube, Christopher L de Graffenried, Jennifer J Kohler. 2006. Regulating cell surface glycosylation with a small-molecule switch.. https://doi.org/10.1016/s0076-6879(06)15014-4

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