Fig. 3
From: Microtubule acetylation dyshomeostasis in Parkinson’s disease
Post-translational modifications of tubulin. The luminal acetylation of K40 and K349 residues of the microtubules (MTs) via α–TAT1 imparts stability to them, and their subsequent deacetylation catalyzed by HDAC6 and SIRT2 makes them unstable by depolymerizing them. Polyglutamylation of tubulin, at the carboxy terminal tail of both tubulin monomers, is a negative regulator of anterograde axonal transport and is governed by the enzymes cytoplasmic carboxypeptidase deglutamylase (CCP) and tubulin tyrosine ligase like (TTLL). Stable tyrosinated MTs are regulated by the enyzyme tubulin tyrosine ligase (TTL) and deregulated to the detyrosinated version via tubulin carboxypeptidase (TCP), which is a complex of vasohibin-1 (VASH1), small vasohibin-binding protein (SVBP) and microtubule-associated tyrosine carboxypeptidase (MATCAP)