Which lipid-linked protein modification is not reversible?
Lipid modifications vary in stability and enzymatic reversibility enabling dynamic membrane association. Palmitoylation S-acylation via DHHC family palmitoyl acyltransferases forming thioester linkage can be removed by acyl protein thioesterases APT1, APT2 and ABHD17 family allowing cycles of membrane binding and cytosolic redistribution crucial for neuronal signaling proteins like PSD-95 and H-Ras. Prenylation thioether linkage is irreversible chemically stable requiring proteolysis for reversal; however protease cleavage of prenylated C-terminus does not regenerate unmodified cysteine. GPI a
Ref: Resh, Nat Chem Biol 2013, Reversibility of lipid modifications; Chamberlain & Shipston, Physiol Rev 2015.
