ATP-citrate lyase promotes axonal transport across species

Aviel Even, Giovanni Morelli, Silvia Turchetto, Michal Shilian, Romain Le Bail, Sophie Laguesse, Nathalie Krusy, Ariel Brisker, Alexander Brandis, Shani Inbar, Alain Chariot, Frédéric Saudou, Paula Dietrich, Ioannis Dragatsis, Bert Brone, Loïc Broix, Jean-Michel Rigo, Miguel Weil () and Laurent Nguyen ()
Additional contact information
Aviel Even: Tel Aviv University
Giovanni Morelli: University of Liège, C.H.U. Sart Tilman
Silvia Turchetto: University of Liège, C.H.U. Sart Tilman
Michal Shilian: Tel Aviv University
Romain Le Bail: University of Liège, C.H.U. Sart Tilman
Sophie Laguesse: University of Liège, C.H.U. Sart Tilman
Nathalie Krusy: University of Liège, C.H.U. Sart Tilman
Ariel Brisker: Tel Aviv University
Alexander Brandis: Life Sciences Core Facilities, Weizmann Institute of Science
Shani Inbar: Tel Aviv University
Alain Chariot: University of Liège, C.H.U. Sart Tilman
Frédéric Saudou: Univ. Grenoble Alpes, Inserm, U1216, CHU Grenoble Alpes, Grenoble Institut Neurosciences
Paula Dietrich: University of Tennessee Health Science Center
Ioannis Dragatsis: University of Tennessee Health Science Center
Bert Brone: BIOMED Research Institute
Loïc Broix: University of Liège, C.H.U. Sart Tilman
Jean-Michel Rigo: BIOMED Research Institute
Miguel Weil: Tel Aviv University
Laurent Nguyen: University of Liège, C.H.U. Sart Tilman

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: Abstract Microtubule (MT)-based transport is an evolutionary conserved process finely tuned by posttranslational modifications. Among them, α-tubulin acetylation, primarily catalyzed by a vesicular pool of α-tubulin N-acetyltransferase 1 (Atat1), promotes the recruitment and processivity of molecular motors along MT tracks. However, the mechanism that controls Atat1 activity remains poorly understood. Here, we show that ATP-citrate lyase (Acly) is enriched in vesicles and provide Acetyl-Coenzyme-A (Acetyl-CoA) to Atat1. In addition, we showed that Acly expression is reduced upon loss of Elongator activity, further connecting Elongator to Atat1 in a pathway regulating α-tubulin acetylation and MT-dependent transport in projection neurons, across species. Remarkably, comparable defects occur in fibroblasts from Familial Dysautonomia (FD) patients bearing an autosomal recessive mutation in the gene coding for the Elongator subunit ELP1. Our data may thus shine light on the pathophysiological mechanisms underlying FD.

Date: 2021
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DOI: 10.1038/s41467-021-25786-y

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