HDAC6 is a microtubule-associated deacetylase

Charlotte Hubbert, Amaris Guardiola, Rong Shao, Yoshiharu Kawaguchi, Akihiro Ito, Andrew Nixon, Minoru Yoshida, Xiao-Fan Wang and Tso-Pang Yao ()
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Charlotte Hubbert: Duke University
Amaris Guardiola: Duke University
Rong Shao: Duke University
Yoshiharu Kawaguchi: The University of Tokyo
Akihiro Ito: Duke University
Andrew Nixon: Duke University
Minoru Yoshida: The University of Tokyo
Xiao-Fan Wang: Duke University
Tso-Pang Yao: Duke University

Nature, 2002, vol. 417, issue 6887, 455-458

Abstract: 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.

Date: 2002
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DOI: 10.1038/417455a

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