Proteomics

Dataset Information

0

S-acylation and fatty acylation in Naïve and LPS/IFN- gamma activated Raw264.7


ABSTRACT: The advances in chemical proteomics have significantly expanded our understanding of the diversity and abundance of fatty-acylated proteins in eukaryotes, and reveal novel functions for these lipid protein modifications. Nonetheless, quantitative comparative proteomic analysis of fatty-acylated proteins in different cellular states is still challenging. To address these limitations, we systematically evaluated different proteomic methods (alk-16 chemical reporter and acyl-RAC) and established robust conditions to selectively and quantitatively profile fatty-acylated proteins in mammalian cells. Using a combination of metabolic labeling with fatty acid chemical reporters, selective chemical enrichment and label-free proteomics, we performed a quantitative analysis of fatty-acylated proteins in naïve and activated macrophages. These studies revealed novel fatty-acylated proteins associated with host immunity that are differently expressed and lipid-modified in different cellular states.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Blood, Macrophage

DISEASE(S): Leukemia

SUBMITTER: Emmanuelle Thinon  

LAB HEAD: Howard C Hang

PROVIDER: PXD003652 | 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]

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