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

Authors

  • Christopher P. Garnham,

    1. Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland
    Search for more papers by this author
  • Antonina Roll-Mecak

    Corresponding author
    1. Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland
    2. National Heart, Lung and Blood Institute, Bethesda, Maryland
    • Cell Biology and Biophysics Unit, Porter Neuroscience Research Center, National Institutes of Health, Building 35, Room 3B-203, 35 Convent Drive, MSC 3700, Bethesda, MD 20892-3700
    Search for more papers by this author

  • Monitoring Editor: Peter Baas

  • This article is a US government work and, as such, is in the public domain in the United States of America.

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. Published 2012 Wiley Periodicals, Inc.

Ancillary