Abstract:Protein palmitoylation is the only fully reversible post-translational lipidation modification for proteins and appears as a ubiquitous mechanism controlling properties and functions of many proteins which exists in physiological processes. Palmitoylation can be achieved by adding long chain lipids into intracellular cysteine residues of soluble transmembrane proteins through unstable thioester bonds. The addition of lipids can increase protein hydrophobicity, which can influence protein structure, assembling, maturation, transportation and function. This review introduces the process of palmitoylation, such as the prediction of palmitoylation sites, the acquisition of palmitoylated proteins, the inhibition of palmitoylation and the use of activators, which brings out the method for combining palmitoylated proteins with mass spectrometry, highlighting the regulatory role of protein function and further discussing its impact on protein transport.
