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Related Experiment Videos

Regulating cell surface glycosylation with a small-molecule switch.

Danielle H Dube1, Christopher L de Graffenried, Jennifer J Kohler

  • 1Department of Chemistry, Stanford University, CA, USA.

Methods in Enzymology
|November 23, 2006
PubMed
Summary
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Researchers developed a novel method to control enzyme activity in the Golgi apparatus using a small molecule. This technique precisely targets glycosyltransferases, essential for glycan epitope formation, by leveraging rapamycin-induced dimerization.

Area of Science:

  • Glycobiology and Cellular Biochemistry
  • Molecular and Cellular Biology
  • Drug Discovery and Chemical Biology

Background:

  • Accurate localization of Golgi-resident enzymes is critical for synthesizing specific glycan structures.
  • Glycosyltransferases, key enzymes in the Golgi, require precise localization for their catalytic function.
  • Existing methods for controlling enzyme activity lack precision in targeting specific Golgi-resident enzymes.

Purpose of the Study:

  • To present a novel method for controlling the localization and activity of individual glycosyltransferases.
  • To utilize a small molecule as an external 'switch' to modulate enzyme function within the Golgi apparatus.
  • To demonstrate the potential of modular enzyme design for targeted biological control.

Main Methods:

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  • Engineered modular glycosyltransferases by separating catalytic and localization domains.
  • Fused these domains to rapamycin-binding proteins (FRB and FKBP) for inducible dimerization.
  • Administered rapamycin to induce dimerization, thereby controlling enzyme localization and activity.

    • Main Results:

    • Successfully demonstrated rapamycin-induced relocalization of engineered glycosyltransferases.
    • Showcased precise control over enzyme activity through external small molecule administration.
    • Validated the modular approach for manipulating Golgi-resident enzyme function.

    Conclusions:

    • The described method provides a powerful tool for precisely controlling glycosyltransferase activity in the Golgi.
    • Rapamycin-mediated dimerization offers a versatile 'switch' for regulating enzyme localization and function.
    • This approach has significant implications for understanding glycan biosynthesis and developing targeted therapeutics.