Quantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of the -acylation machinery.

Protein palmitoylation or -acylation has emerged as a key regulator of cellular processes. Increasing evidence shows that this modification is not restricted to palmitate but it can include additional fatty acids, raising the possibility that differential -acylation contributes to the fine-tuning of protein activity. However, methods to profile the acyl moieties attached to proteins are scarce.

Palmitoylation as a Key Regulator of Ras Localization and Function.

Ras proteins require membrane association for proper function. This process is tightly regulated by reversible palmitoylation that controls not only the distribution over different subcellular compartments but also Ras compartmentalization within membrane subdomains. As a result, there is a growing interest in protein palmitoylation and the enzymes that control this process.