Regulating Cell Surface Glycosylation with a Small-Molecule Switch

Danielle H. Dube, Christopher L. de Graffenried, Jennifer J. Kohler

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)213-229
Number of pages17
JournalMethods in Enzymology
StatePublished - 2006

ASJC Scopus subject areas

  • Biochemistry


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