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.