Dataset Information

S-acylated and S-palmitoylated proteins in HeLa

ABSTRACT: S-fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryotes and is important in mammalian physiology and human disease. While chemical labeling methods have improved the detection and enrichment of S-fatty-acylated proteins, mapping sites of modification and characterization of endogenously attached fatty acids is still challenging. here, we optimized and compared two methods widely employed to identify S-fatty-acylated proteins by MS-based proteomics. While these methods identified an overlapping list of fatty-acylated proteins, only alk-16 chemical reporter combined with NH2OH specifically and robustly identified S-fatty-acylated proteins. Alk-16 chemical reporter labeling alone gave a list of S/N/O-fatty acylated proteins, while acyl-RAC provided a list of S-acylated proteins. Acyl-RAC identifies any proteins with a thioester modification and is often misused in the literature to validate S-fatty-acylated proteins. It would be preferable, when validating new S-fatty-acylated proteins, to use acyl-RAC and alk-16 (+/-NH2OH) in combination.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Emmanuelle Thinon

LAB HEAD: Howard C Hang

PROVIDER: PXD008398 | Pride | 2018-03-28

REPOSITORIES: Pride

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Publications

Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.

Thinon Emmanuelle E Fernandez Joseph P JP Molina Henrik H Hang Howard C HC

Journal of proteome research 20180406 5

S-Fatty-acylation is the covalent attachment of long chain fatty acids, predominately palmitate (C16:0, S-palmitoylation), to cysteine (Cys) residues via a thioester linkage on proteins. This post-translational and reversible lipid modification regulates protein function and localization in eukaryotes and is important in mammalian physiology and human diseases. While chemical labeling methods have improved the detection and enrichment of S-fatty-acylated proteins, mapping sites of modification a ...[more]

PMID: 29575903

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Dataset Information

S-acylated and S-palmitoylated proteins in HeLa

Publications

Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.

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