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Article Dans Une Revue Current Biology - CB Année : 2017

Causes and Consequences of Microtubule Acetylation

Résumé

Among the different types of cytoskeletal components, microtubules arguably accumulate the greatest diversity of post-translational modifications (PTMs). Acetylation of lysine 40 (K40) of atubulin has received a particular attention because it is the only tubulin PTM to be found in the lumen of microtubules - most other tubulin PTMs are found at their outer surface. As a consequence, the enzyme catalyzing K40 acetylation needs to penetrate the narrow microtubules lumen to find its substrate. Acetylated microtubules have been considered as stable, long-lived microtubules, however until recently there was little information about whether the longevity of these microtubules is the cause or the consequence of acetylation. Current advances suggest that this PTM helps the microtubule lattice to cope with mechanical stress, thus facilitating microtubule self-repair. These observations now shed a new light on the structural integrity of microtubules, as well as on mechanisms and biological functions of tubulin acetylation. Here we discuss the recent understanding on how acetylation is generated in the lumen of microtubules, and how this ‘hidden’ PTM can control microtubule properties and functions.
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Dates et versions

hal-02375830 , version 1 (03-12-2019)

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Carsten Janke, Guillaume Montagnac. Causes and Consequences of Microtubule Acetylation. Current Biology - CB, 2017, ⟨10.1016/j.cub.2017.10.044⟩. ⟨hal-02375830⟩
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