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

2012/03/15 by Christopher P. Garnham, Antonina Roll‐Mecak · 1 citation
Biochemistry, Genetics and Molecular Biology · #Microtubule and mitosis dynamics #Ubiquitin and proteasome pathways #14-3-3 protein interactions

paper · pdf · doi:10.1002/cm.21027

openalex publication_date 2012/03/15 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/15

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.

Citations

• Posttranslational Glutamylation of α-tubulin
• Reversible polyglutamylation of alpha- and beta-tubulin and microtubule dynamics in mouse brain neurons.
• HDAC6 is a microtubule-associated deacetylase
• Low expression of human tubulin tyrosine ligase and suppressed tubulin tyrosination/detyrosination cycle are associated with impaired neuronal differentiation in neuroblastomas with poor prognosis
• Characterization of the tubulin-tyrosine ligase.
• The carboxypeptidase-like substrate-binding site in Nna1 is essential for the rescue of the Purkinje cell degeneration (pcd) phenotype
• Translating the Histone Code
• Role of kinesin-1 and cytoplasmic dynein in endoplasmic reticulum movement in VERO cells

Cited by

• Microtubule [wikipedia]