Skip to main content
. Author manuscript; available in PMC: 2015 Mar 1.
Published in final edited form as: Medchemcomm. 2014 Mar;5(3):268–276. doi: 10.1039/C3MD00333G

Figure 1. A dynamic S-palmitoylation cycle regulates the membrane association and activity of certain palmitoylated proteins.

Figure 1

Certain stimuli cause an acyl protein thioesterase to catalyze thioester hydrolysis of palmitoylated cysteine residues. De-palmitoylation liberates the protein from the plasma membrane, allowing it to segregate to the cytosol disrupting interactions with membrane-associated signaling complexes. The protein can then undergo re-palmitoylation by Golgi-resident DHHC palmitoyl transferases, transport back to the plasma membrane, and re-associate with signaling partners.