| Modification Notes |
Polyglutamylation, polyglycylation and tyrosination are posttransational modifications that tubulin undergoes in order to perform at maximal function. Polyglutamylation is evolutionarily conserved from protists to mammals and is involved in several microtubule functions such as axonemal beating, stability of centrioles, neuronal differentiation and mediating the interaction between tubulin and microtubule associated proteins. The neuronal tubulin polyglutamylase is a complex that contains a TTL (tubulin tyrosine ligase-like) domain through which it catalyzes the ligation of glutamate to tubulins. The TTL domain contains ATP-grasp-like motifs that correspond to the ATP/Mg(2+) binding site typical of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. PGs2 (Tubulin polyglutamylase complex subunit 2), also known as C18orf10, is a 300 amino acid cytoplasmic protein that participates in the neuronal tubulin polyglutamylase complex, along with PGs1, PGs3, PGs4 and PGs5. There are two isoforms of PGs2 that are produced as a reslt of alternative splicing events. |