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Journal Articles Nature Year : 2013

αTAT1 catalyses microtubule acetylation at clathrin-coated pits

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Abstract

In most eukaryotic cells microtubules undergo post-translational modifications such as acetylation of α-tubulin on lysine 40, a widespread modification restricted to a subset of microtubules that turns over slowly1. This subset of stable microtubules accumulates in cell protrusions2 and regulates cell polarization3, migration and invasion4,5,6,7. However, mechanisms restricting acetylation to these microtubules are unknown. Here we report that clathrin-coated pits (CCPs) control microtubule acetylation through a direct interaction of the α-tubulin acetyltransferase αTAT1 (refs 8, 9) with the clathrin adaptor AP2. We observe that about one-third of growing microtubule ends contact and pause at CCPs and that loss of CCPs decreases lysine 40 acetylation levels. We show that αTAT1 localizes to CCPs through a direct interaction with AP2 that is required for microtubule acetylation. In migrating cells, the polarized orientation of acetylated microtubules correlates with CCP accumulation at the leading edge10, and interaction of αTAT1 with AP2 is required for directional migration. We conclude that microtubules contacting CCPs become acetylated by αTAT1. In migrating cells, this mechanism ensures the acetylation of microtubules oriented towards the leading edge, thus promoting directional cell locomotion and chemotaxis.

Dates and versions

pasteur-03721554 , version 1 (12-07-2022)

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Guillaume Montagnac, Vannary Meas-Yedid, Marie Irondelle, Antonio Castro-Castro, Michel Franco, et al.. αTAT1 catalyses microtubule acetylation at clathrin-coated pits. Nature, 2013, 502 (7472), pp.567-570. ⟨10.1038/nature12571⟩. ⟨pasteur-03721554⟩
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