Palmitoylation

Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments,[3] as well as in modulating protein–protein interactions.

Because palmitoylation is a dynamic, post-translational process, it is believed to be employed by the cell to alter the subcellular localization, protein–protein interactions, or binding capacities of a protein.

An example of a protein that undergoes palmitoylation is hemagglutinin, a membrane glycoprotein used by influenza to attach to host cell receptors.

[5] The palmitoylation cycles of a wide array of enzymes have been characterized in the past few years, including H-Ras, Gsα, the β2-adrenergic receptor, and endothelial nitric oxide synthase (eNOS).

It runs on a ping-pong mechanism, where the cysteine attacks the acyl-CoA to form an S-acylated DHHC, and then the acyl group is transferred to the substrate.

Scientists have appreciated the significance of attaching long hydrophobic chains to specific proteins in cell signaling pathways.

Also, in the presynaptic neuron, palmitoylation of SNAP-25 directs it to partition in the cell membrane [17] and allows the SNARE complex to dissociate during vesicle fusion.

[18] Palmitoylation of delta catenin seems to coordinate activity-dependent changes in synaptic adhesion molecules, synapse structure, and receptor localizations that are involved in memory formation.