Suppression of tubulin tyrosine ligase activity through reversible phosphorylation: a mechanism for inhibition of alpha-tubulin tyrosinylation.
The tubulin tyrosinylation/detyrosinylation cycle is a well-established posttranslational modification, which is carried out by two enzymes: tubulin tyrosine ligase (TTL) and tubulin tyrosine carboxypeptidase (TTCP). In this paper, I present evidence suggesting that the cycle itself is under the hierarchical control of reversible phosphorylation and that proteinkinase C (PKC)-mediated phosphorylation of TTL inhibits its activity, thereby preventing tubulin tyrosinylation. Phosphorylation of TTL is postulated to occur in its presumed Mg(++)-ATP binding fold, leading to inhibition of Mg(++)/ATP binding and TTL mediated catalysis. The implications of such control are also discussed. Copyright 2001 Harcourt Publishers Ltd.
Idriss
H. T.
HT
School of Biomedical Sciences, University of St Andrews, St Andrews, UK