Detection of Heterogeneous Protein S-Acylation in Cells

Jennifer Greaves, Nicholas C O Tomkinson

    Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

    Abstract

    The use of synthetically synthesized azide and alkyne fatty acid analogs coupled with bioorthogonal Cu(I)-catalyzed Huisgen 1,3-dipolar cycloaddition reaction-based detection methods to study protein S-acylation reactions has replaced the traditional method of using in vivo metabolic radiolabeling with tritiated palmitic acid and has greatly facilitated our understanding of this essential cellular process. Here, we describe the chemical synthesis of myristic (C:14), palmitic (C16:0), and stearic (C18:0) acid-azide probes and detail how they may be utilized as chemical reporters for the analysis of S-acylation of exogenously expressed proteins in cells.

    Original languageEnglish
    Title of host publicationProtein Lipidation
    EditorsM.E Linder
    PublisherSpringer
    Chapter2
    Pages13-33
    Number of pages21
    ISBN (Electronic)978-1-4939-9532-5
    ISBN (Print)978-1-4939-9531-8
    DOIs
    Publication statusPublished - 1 Jun 2019

    Publication series

    NameMethods in Molecular Biology
    Volume2009
    ISSN (Print)1064-3745
    ISSN (Electronic)1940-6029

    Keywords

    • Click chemistry
    • Fatty acid azide
    • Fatty acylation
    • Palmitoylation
    • S-Acylation

    ASJC Scopus subject areas

    • Molecular Biology
    • Genetics

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