Stabilization of post-translational modification of microtubules during cellular morphogenesis

Bioessays. 1991 Jun;13(6):285-93. doi: 10.1002/bies.950130605.


This review discusses the possible role of alpha-tubulin detyrosination, a reversible post-translational modification that occurs at the protein's C-terminus, in cellular morphogenesis. Higher eukaryotic cells possess a cyclic post-translational mechanism by which dynamic microtubules are differentiated from their more stable counterparts; a tubulin-specific carboxypeptidase detyrosinates tubulin protomers within microtubules, while the reverse reaction, tyrosination, is performed on the soluble protomer by a second tubulin-specific enzyme, tubulin tyrosine ligase. In general, the turnover of microtubules in undifferentiated, proliferating cells is so rapid that the microtubules accumulate very little detyrosinated tubulin; that is, they are enriched in tyrosinated tubulin. However, an early event common to at least three well-studied morphogenetic events--myogenesis, neuritogenesis, and directed cell motility--is the elaboration of a polarized array of stable microtubules that become enriched in detyrosinated tubulin. The formation of this specialized array of microtubules in specific locations in cells undergoing morphogenesis suggests that it plays an important role in generating cellular asymmetries.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Carboxypeptidases / metabolism
  • Cell Differentiation
  • Cell Movement
  • Eukaryotic Cells / metabolism
  • Eukaryotic Cells / ultrastructure*
  • Microtubules / metabolism*
  • Microtubules / ultrastructure
  • Morphogenesis
  • Peptide Synthases / metabolism
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Protein-Tyrosine Kinases / metabolism
  • Tubulin / metabolism*


  • Tubulin
  • Protein-Tyrosine Kinases
  • Carboxypeptidases
  • Peptide Synthases
  • tyrosyltubulin ligase