InterPro domain: IPR004344

Tubulins and microtubules are subjected to several post-translational modifications of the carboxy-terminal end of most major forms of tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL) and the tubulin polyglutamylase (TTLL) [ 1 , 2 ]. Tubulin-tyrosine ligase (TTL) catalyses the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. Tubulin polyglutamylase (such as TTLL10) can modify both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins [ 3 ]. Tubulin polyglutamylation may be involved in the organisation of the neuronal microtubule network, in centriole stability, axoneme motility and mitosis [ 3 ].

1. Tubulin-tyrosine ligase, a long-lasting enigma. Neurochem. Res. 25, 5-10
2. Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell 137, 1076-87
3. Tubulin polyglutamylase enzymes are members of the TTL domain protein family. Science 308, 1758-62