What does S Palmitoylation do to membrane proteins?
By controlling the association of membrane proteins with specific membrane domains/compartments, palmitoylation can bring together, or alternatively segregate, proteins that have the ability to interact under specific circumstances. It could be due to the affinity of palmitate for specific lipids or lipid domains.
What is palmitoylation and what is it used for in the cell?
Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments, as well as in modulating protein–protein interactions.
How do you inhibit palmitoylation?
The lipid-based palmitoylation inhibitors include compounds such as 2BP, cerulenin and tunicamycin, and have been used to inhibit palmitoylation in vitro and in cells.
Why is palmitoylation reversible?
Compared to the other lipid modifications, palmitoylation is readily reversible due to the lability of the thioester bond. Therefore rapid cycles of palmitoylation and depalmitoylation allow proteins to be facilely shuttled between the plasma membrane and the Golgi apparatus to regulate many cellular functions (29–35).
Is palmitoylation post-translational modification?
S-palmitoylation is a reversible lipid post-translational modification, involved in different biological processes, such as the trafficking of membrane proteins, achievement of stable protein conformations, and stabilization of protein interactions.
Where does myristoylation happen?
Myristoylation has been found to occur on penultimate N-terminal glycine residues and requires the prior removal of the initial methionine residue. This myristoylation is an early event in acyl protein biosynthesis and can be blocked immediately by inhibiting protein biosynthesis (Olson and Spizz, 1986).