The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions

Cytoskeleton (Hoboken). 2012 Jul;69(7):442-63. doi: 10.1002/cm.21027. Epub 2012 Apr 26.

Abstract

Cellular microtubules are marked by abundant and evolutionarily conserved post-translational modifications that have the potential to tune their functions. This review focuses on the astonishing chemical complexity introduced in the tubulin heterodimer at the post-translational level and summarizes the recent advances in identifying the enzymes responsible for these modifications and deciphering the consequences of tubulin's chemical diversity on the function of molecular motors and microtubule associated proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Humans
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / enzymology*
  • Microtubules / genetics
  • Models, Molecular
  • Protein Processing, Post-Translational*
  • Tubulin / chemistry
  • Tubulin / genetics
  • Tubulin / metabolism*

Substances

  • Microtubule-Associated Proteins
  • Tubulin