Abstract
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 language | English (US) |
|---|---|
| Title of host publication | Mass Spectrometry-Based Chemical Proteomics |
| Publisher | Wiley |
| Pages | 317-347 |
| Number of pages | 31 |
| ISBN (Electronic) | 9781118970195 |
| ISBN (Print) | 9781118969557 |
| DOIs | |
| State | Published - Jan 1 2019 |
Bibliographical note
Publisher Copyright:© 2019 John Wiley & Sons, Inc.
Keywords
- Chemical proteomic approach
- Cholesterol analogs
- Fatty acylation
- Glycosylphosphatidyl-inositol anchors
- Metabolic labeling
- Plasmodium falciparum
- Prenylation
- Protein-lipid modifications
