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Related Experiment Videos

A small-molecule switch for Golgi sulfotransferases.

Christopher L de Graffenried1, Scott T Laughlin, Jennifer J Kohler

  • 1Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 19, 2004
PubMed
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Researchers developed a novel system to control Golgi-resident sulfotransferases using a chemical inducer. This method allows for the study of glycan function and sulfate-dependent biological processes.

Area of Science:

  • Glycobiology
  • Chemical Biology
  • Enzymology

Background:

  • Glycan function is crucial in biology, and sulfotransferases play a key role in modulating these functions.
  • Targeting sulfotransferases with small molecules is a promising strategy for studying glycan roles.
  • Existing methods lack precise control over sulfotransferase activity in cellular environments.

Purpose of the Study:

  • To develop a system for conditional activation of Golgi-resident sulfotransferases.
  • To enable the study of sulfate-dependent biological processes using small molecules.
  • To demonstrate the versatility of this system for other Golgi-resident enzymes.

Main Methods:

  • Engineered fusion proteins combining sulfotransferase catalytic domains with FKBP or FRB domains.

Related Experiment Videos

  • Utilized rapamycin, a chemical inducer of dimerization, to conditionally activate enzyme activity.
  • Applied the system to GlcNAc-6-sulfotransferases (GlcNAc6ST-1 and GlcNAc6ST-2) involved in L-selectin ligand sulfation.
  • Created chimeric enzymes with domains from different Golgi enzymes to test system generality.

    • Main Results:

    • Achieved conditional activation of Golgi-resident sulfotransferases using rapamycin.
    • Demonstrated that the inducible enzymes exhibit activity and specificity comparable to wild-type enzymes.
    • Successfully generated rapamycin-inducible chimeric enzymes, showcasing the system's broad applicability to other Golgi enzymes.
    • Validated the system's efficacy in studying L-selectin ligand sulfation.

    Conclusions:

    • The developed chemical induction system provides precise temporal control over Golgi-resident sulfotransferase activity.
    • This approach facilitates the investigation of sulfate-dependent biological processes in cellular contexts and potentially in vivo.
    • The modularity of the system allows for its application to a range of Golgi enzymes, advancing glycobiology research.