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ATP-citrate lyase promotes axonal transport across species

Author

Listed:
  • Aviel Even

    (Tel Aviv University)

  • Giovanni Morelli

    (University of Liège, C.H.U. Sart Tilman
    BIOMED Research Institute)

  • 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
    Inserm, U1216
    CHU Grenoble Alpes)

  • 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)

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.

Suggested Citation

  • Aviel Even & Giovanni Morelli & Silvia Turchetto & Michal Shilian & Romain Le Bail & Sophie Laguesse & Nathalie Krusy & Ariel Brisker & Alexander Brandis & Shani Inbar & Alain Chariot & Frédéric Saudo, 2021. "ATP-citrate lyase promotes axonal transport across species," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25786-y
    DOI: 10.1038/s41467-021-25786-y
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    References listed on IDEAS

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