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Marginal band microtubules are acetylated by αTAT1

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Version 2 2020-08-22, 02:31
Version 1 2020-05-02, 16:36
journal contribution
posted on 2020-08-22, 02:31 authored by Anne-Sophie Ribba, Morgane Batzenschlager, Clotilde Rabat, Thierry Buchou, Sylvie Moog, Saadi Khochbin, Ekaterina Bourova-Flin, Laurence Lafanechère, François Lanza, Karin Sadoul

The discoid shape of resting platelets is maintained by a peripheral, circular bundle of microtubules called marginal band. Marginal band microtubules are acetylated on lysine 40 of the alpha-tubulin subunits. We have previously shown that the deacetylase HDAC6 is responsible for tubulin deacetylation in platelets and that the hyperacetylated state of the microtubules in HDAC6KO platelets correlates with faster activation/spreading kinetics, pointing to a regulatory role of this modification. So far, the question about the reverse enzyme, responsible for tubulin acetylation in platelets, has remained unanswered. Several enzymes have been described as having tubulin acetylation activity. Here we identify αTAT1 as the enzyme responsible for the acetylation of marginal band microtubules. We show that αTAT1 deficiency has only minor consequences for platelet production and function. A residual tubulin acetylation level in αTAT1 deficient platelet lysates suggests the presence of an additional tubulin-acetylating enzyme that is unable to acetylate marginal band microtubules.

Funding

This work was supported by the Fondation Recherche Médicale (FRM, grant number DEI20151234416) and the University Grenoble Alpes (UGA, grant number AGIR-POLE FRAG15CS08) as well as by funds from the Association de Recherche et Développement en Médecine et Santé Publique (ARMESA to M.B.).

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