TY - JOUR
T1 - Regulating Cell Surface Glycosylation with a Small-Molecule Switch
AU - Dube, Danielle H.
AU - de Graffenried, Christopher L.
AU - Kohler, Jennifer J.
PY - 2006
Y1 - 2006
N2 - 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.
AB - 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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U2 - 10.1016/S0076-6879(06)15014-4
DO - 10.1016/S0076-6879(06)15014-4
M3 - Article
C2 - 17116477
AN - SCOPUS:33751005265
SN - 0076-6879
VL - 415
SP - 213
EP - 229
JO - Methods in Enzymology
JF - Methods in Enzymology
ER -