Protein Lipidation by Palmitoylation and Myristoylation in Cancer

Posttranslational modification of proteins with lipid moieties is known as protein lipidation. The attachment of a lipid molecule to proteins endows distinct properties, which affect their hydrophobicity, structural stability, localization, trafficking between membrane compartments, and influences its interaction with effectors. Lipids or lipid metabolites can serve as substrates for lipidation, and the availability of these lipid substrates are tightly regulated by cellular metabolism. Palmitoylation and myristoylation represent the two most common protein lipid modifications, and dysregulation of protein lipidation is strongly linked to various diseases such as metabolic syndromes and cancers. In this review, we present recent developments in our understanding on the roles of palmitoylation and myristoylation, and their significance in modulating cancer metabolism toward cancer initiation and progression.

Automated summary

Protein lipidation, a posttranslational modification involving lipid moieties, plays a crucial role in modulating the properties and interactions of proteins, closely linked to cellular metabolism. The two most common protein lipid modifications, palmitoylation and myristoylation, have significant implications in regulating cancer metabolism and progression. Dysregulation of protein lipidation is strongly associated with various diseases, highlighting the importance of understanding its roles in health and disease.