Proteomic analysis of protein-lipid modifications: Significance and application

Kiall F. Suazo, Garrett Schey, Chad Schaber, Audrey R.Odom John, Mark D. Distefano

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations


Post-translational modifications are key players in the regulation of biological function of proteins, as well as modulators of activity and cellular localization. In particular, protein lipid modification is essential for both stable anchoring of proteins to membranes and protein trafficking. The currently known lipidations include myristoylation, palmitoylation, prenylation, cholesterylation, and glycosylphosphatidyl-inositol anchors. In this chapter, results from a variety of proteomic analysis using metabolic labeling in conjunction with enrichment are described for the different lipid modifications. That is followed by a detailed description for how such analyses are performed for one example where the prenylated proteins from Plasmodium falciparum, the causative agent for malaria, were identified.

Original languageEnglish (US)
Title of host publicationMass Spectrometry-Based Chemical Proteomics
Number of pages31
ISBN (Electronic)9781118970195
ISBN (Print)9781118969557
StatePublished - Jan 1 2019

Bibliographical note

Publisher Copyright:
© 2019 John Wiley & Sons, Inc.


  • Chemical proteomic approach
  • Cholesterol analogs
  • Fatty acylation
  • Glycosylphosphatidyl-inositol anchors
  • Metabolic labeling
  • Plasmodium falciparum
  • Prenylation
  • Protein-lipid modifications


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