Quantification of Protein Palmitoylation by Cysteine-SILAC

Caiyun Fang; Xiaoqin Zhang; Haojie Lu

doi:10.1007/978-1-0716-2863-8_5

Quantification of Protein Palmitoylation by Cysteine-SILAC

Methods Mol Biol. 2023:2603:59-69. doi: 10.1007/978-1-0716-2863-8_5.

Authors

Caiyun Fang¹, Xiaoqin Zhang², Haojie Lu³

Affiliations

¹ Department of Chemistry, Fudan University, Shanghai, China. fangcaiyun@fudan.edu.cn.
² Department of Pharmaceutics, College of Medicine, Jiaxing University, Jiaxing, China.
³ Department of Chemistry and Institutes of Biomedical Sciences, Fudan University, Shanghai, China. luhaojie@fudan.edu.cn.

PMID: 36370270
DOI: 10.1007/978-1-0716-2863-8_5

Abstract

Cysteine-SILAC enables the detection and quantification of protein S-palmitoylation, an important protein posttranslational modification. Here we describe the cell culture, protein extraction, selective enrichment, mass spectrometry, and data analysis for palmitoylated proteins from cell samples by this method.

Keywords: Cysteine-SILAC; Mass spectrometry; Metabolic labeling; Protein palmitoylation; Selective enrichment.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cysteine* / metabolism
Lipoylation*
Mass Spectrometry
Protein Processing, Post-Translational
Proteins / metabolism

Substances

Cysteine
Proteins