Detection of Heterogeneous Protein S-Acylation in Cells

Jennifer Greaves, Nicholas C O Tomkinson

Research output: Chapter in Book/Report/Conference proceedingChapter

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

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Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Greaves, J., & Tomkinson, N. C. O. (2019). Detection of Heterogeneous Protein S-Acylation in Cells. In M. E. Linder (Ed.), Protein Lipidation (pp. 13-33). (Methods in Molecular Biology; Vol. 2009). Springer. https://doi.org/10.1007/978-1-4939-9532-5_2