Long, short and medium chain fatty acids are covalently attached to hundreds of proteins.
Each fatty acid confers distinct biochemical properties, enabling fatty acylation to regulate …

INTRODUCTION Hundreds of cellular proteins are modified by posttranslational S-acylation
of cysteines, commonly known as protein palmitoylation. Unlike other lipid attachments …

Protein palmitoylation refers to the posttranslational addition of a 16 carbon fatty acid to the
side chain of cysteine, forming a thioester linkage. This acyl modification is readily …

Although palmitoylation regulates numerous cellular processes, as yet efforts to manipulate
this post-translational modification for therapeutic gain have proved unsuccessful. The Na …

Protein S-palmitoylation, the most common lipid modification with the 16-carbon fatty acid
palmitate, provides an important mechanism for regulating protein trafficking and function …

Protein S-palmitoylation, the covalent lipid modification of the side chain of Cys residues
with the 16-carbon fatty acid palmitate, is the most common acylation of proteins in …

Highlights•Protein fatty-acylation regulates many fundamental biological processes in
eukaryotes.•Chemical proteomics has expanded the potential functions of protein fatty …

Posttranslational modifications, including phosphorylation, ubiquitination and lipid
modifications, provide proteins with additional functions and regulation beyond genomic …

Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid
chain is covalently linked to cysteine residues by a thioester linkage. A family of integral …

Posttranslational modification provides proteins with additional function and regulatory
control beyond genomic information, allowing cells to maintain homeostasis and respond to …