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HDAC6 is a microtubule-associated deacetylase

Author

Listed:
  • Charlotte Hubbert

    (Duke University)

  • Amaris Guardiola

    (Duke University)

  • Rong Shao

    (Duke University)

  • Yoshiharu Kawaguchi

    (The University of Tokyo
    Japan Science and Technology Corporation)

  • Akihiro Ito

    (Duke University)

  • Andrew Nixon

    (Duke University)

  • Minoru Yoshida

    (The University of Tokyo
    Japan Science and Technology Corporation)

  • Xiao-Fan Wang

    (Duke University)

  • Tso-Pang Yao

    (Duke University)

Abstract

Reversible acetylation of α-tubulin has been implicated in regulating microtubule stability and function1. The distribution of acetylated α-tubulin is tightly controlled and stereotypic. Acetylated α-tubulin is most abundant in stable microtubules but is absent from dynamic cellular structures such as neuronal growth cones and the leading edges of fibroblasts1,2. However, the enzymes responsible for regulating tubulin acetylation and deacetylation are not known. Here we report that a member of the histone deacetylase family, HDAC6, functions as a tubulin deacetylase. HDAC6 is localized exclusively in the cytoplasm, where it associates with microtubules and localizes with the microtubule motor complex containing p150glued (ref. 3). In vivo, the overexpression of HDAC6 leads to a global deacetylation of α-tubulin, whereas a decrease in HDAC6 increases α-tubulin acetylation. In vitro, purified HDAC6 potently deacetylates α-tubulin in assembled microtubules. Furthermore, overexpression of HDAC6 promotes chemotactic cell movement, supporting the idea that HDAC6-mediated deacetylation regulates microtubule-dependent cell motility. Our results show that HDAC6 is the tubulin deacetylase, and provide evidence that reversible acetylation regulates important biological processes beyond histone metabolism and gene transcription.

Suggested Citation

  • Charlotte Hubbert & Amaris Guardiola & Rong Shao & Yoshiharu Kawaguchi & Akihiro Ito & Andrew Nixon & Minoru Yoshida & Xiao-Fan Wang & Tso-Pang Yao, 2002. "HDAC6 is a microtubule-associated deacetylase," Nature, Nature, vol. 417(6887), pages 455-458, May.
  • Handle: RePEc:nat:nature:v:417:y:2002:i:6887:d:10.1038_417455a
    DOI: 10.1038/417455a
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    Cited by:

    1. 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.
    2. Caroline Dour & Maria Chatzifrangkeskou & Coline Macquart & Maria M. Magiera & Cécile Peccate & Charlène Jouve & Laura Virtanen & Tiina Heliö & Katriina Aalto-Setälä & Silvia Crasto & Bruno Cadot & Dé, 2022. "Actin-microtubule cytoskeletal interplay mediated by MRTF-A/SRF signaling promotes dilated cardiomyopathy caused by LMNA mutations," Nature Communications, Nature, vol. 13(1), pages 1-21, December.
    3. Mireia Andreu-Carbó & Cornelia Egoldt & Marie-Claire Velluz & Charlotte Aumeier, 2024. "Microtubule damage shapes the acetylation gradient," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    4. Patricia González-Rodríguez & Daniel J. Klionsky & Bertrand Joseph, 2022. "Autophagy regulation by RNA alternative splicing and implications in human diseases," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    5. Josep J Centelles, 2019. "Microtubule Stabilization by Drugs or Enzymes," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 22(2), pages 16477-16479, October.

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