Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualization, identification and quantification ofN-myristoylation,N- andS-acylation,O-cholesterylation,S-farnesylation andS-geranylgeranylation

Wouter W. Kallemeijn, Thomas Lanyon-Hogg, Nattawadee Panyain, Andrea Goya Grocin, Paulina Ciepla, Julia Morales-Sanfrutos, Edward W. Tate

Published: 2021-10-26 DOI: 10.1038/s41596-021-00601-6

Protein lipidation

Chemical proteomics

Quantitative mass spectrometry

In-gel fluorescence

Lipid PTMs

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Protein lipidation is one of the most widespread post-translational modifications (PTMs) found in nature, regulating protein function, structure and subcellular localization. Lipid transferases and their substrate proteins are also attracting increasing i
Introduction
Materials
Procedure 1: in-gel fluorescence visualization of lipid probe–nobreaklabeled proteins
Procedure 2: identification and quantification of lipid PTMs by chemical proteomics
Troubleshooting
Anticipated results
References
ACKNOWLEDGMENTS

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Proteome-wide analysis of protein lipidation using chemical probes: in-gel fluorescence visualization, identification and quantification ofN-myristoylation,N- andS-acylation,O-cholesterylation,S-farnesylation andS-geranylgeranylation

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