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Review
. 2008 Feb;20(1):71-6.
doi: 10.1016/j.ceb.2007.11.010. Epub 2008 Jan 15.

Tubulin modifications and their cellular functions

Jennetta W Hammond  1 , Dawen Cai, Kristen J Verhey
Affiliations
Review

Tubulin modifications and their cellular functions

Jennetta W Hammond et al. Curr Opin Cell Biol. 2008 Feb.

Abstract

All microtubules are built from a basic alpha/beta-tubulin building block, yet subpopulations of microtubules can be differentially marked by a number of post-translational modifications. These modifications, conserved throughout evolution, are thought to act individually or in combination to control specific microtubule-based functions, analogous to how histone modifications regulate chromatin functions. Here we review recent studies demonstrating that tubulin modifications influence microtubule-associated proteins such as severing proteins, plus-end tracking proteins, and molecular motors. In this way, tubulin modifications play an important role in regulating microtubule properties, such as stability and structure, as well as microtubule-based functions, such as ciliary beating, cell division, and intracellular trafficking.

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Figures

Figure 1
Figure 1. Localization of microtubule structures and modified tubulin subunits in mammalian cells
(a) In interphase cells, dynamic microtubules (orange) lack PTMs whereas stable microtubules (red) accumulate PTMs in a time-dependent manner. Ciliary microtubules (green) contain PTMs primarily on the B tubule of the outer doublets. Note that motile cilia contain the 9+2 arrangement of nine doublet microtubules around a central pair (shown) whereas primary cilia lack the central pair (9+0, not shown). PTMs are also prevalent in centriolar/basal body triplet microtubules (yellow). (b) In mitotic cells, spindle microtubules (kinetochore and/or interpolar) microtubules are highly modified whereas astral microtubules are mostly unmodified.
Figure 2
Figure 2. Localization of tubulin PTMs on the α/β-tubulin heterodimer
Microtubules are formed by the end-on-end and lateral associations of α- (green) and β- (blue) tubulin heterdimers. The crystal structure (PDB file 1TUB) of one tubulin heterodimer is shown. The CTTs of both α- and β-tubulin, disordered in the structure, are represented in this schematic as dashed lines. Detyrosination entails the removal of the C-terminal tyrosine (Y) from α-tubulin. The resulting detyrosinated α-tubulin is often referred to as Glu tubulin due to the exposed glutamate residue. Polyglutamylation (EEE) and polyglycylation (GGG) occur on the CTTs of α- and β-tubulin. Acetylation of α-tubulin occurs on lysine40 (K40) which is predicated to lie on the luminal face of the microtubule.
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References

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    1. Reed NA, Cai D, Blasius TL, Jih GT, Meyhofer E, Gaertig J, Verhey KJ. Microtubule acetylation promotes kinesin-1 binding and transport. Curr Biol. 2006;16:2166–2172. This paper showed that transport of JIP1, a Kinesin-1 cargo, is directed to only a subset of neurites in neuronal cells. The mechanism of polarized trafficking depends on tubulin PTMs as hyperacetylation redirected JIP1 transport to nearly all neurites and Kinesin-1 binds with higher affinity to acetylated microtubules.

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