Marginal band microtubules are acetylated by αTAT1

Autor: Anne-Sophie Ribba, Laurence Lafanechère, Morgane Batzenschlager, Ekaterina Bourova-Flin, Clotilde Rabat, Karin Sadoul, François Lanza, Saadi Khochbin, Thierry Buchou, Sylvie Moog
Přispěvatelé: Khochbin, Saadi, Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Universitaire [Grenoble] (CHU)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Platelets
Platelets, Taylor & Francis, 2020
ISSN: 0953-7104
1369-1635
Popis: International audience; 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.
Databáze: OpenAIRE