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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

Oncogene volume 26, pages 5468–5476 (2007)Cite this article

Abstract

Histone deacetylase 6 (HDAC6) is a unique enzyme with specific structural and functional features. It is actively or stably maintained in the cytoplasm and is the only member, within the histone deacetylase family, that harbors a full duplication of its deacetylase homology region followed by a specific ubiquitin-binding domain at the C-terminus end. Accordingly, this deacetylase functions at the heart of a cellular regulatory mechanism capable of coordinating various cellular functions largely relying on the microtubule network. Moreover, HDAC6 action as a regulator of the HSP90 chaperone activity adds to the multifunctionality of the protein, and allows us to propose a critical role for HDAC6 in mediating and coordinating various cellular events in response to different stressful stimuli.

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Acknowledgements

We gratefully acknowledge the association ‘vaincre la mucoviscidose’ for supporting CB PhD fellowship for 4 years and Dr Sophie Rousseaux for critical reading of the manuscript. SK laboratory was supported by CLARA cancéropôle, EpiMed and INCa EpiPro and Association pour la Recherche sur le Cancer (ARC) ARECA programs.

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  1. INSERM, U823, Equipe Epigénétique et Signalisation Cellulaire, Institut Albert Bonniot, Université Joseph Fourier, Domaine de la Merci, Grenoble, La Tronche Cedex, France

    C Boyault, K Sadoul, M Pabion & S Khochbin

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Boyault, C., Sadoul, K., Pabion, M. et al. HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination. Oncogene 26, 5468–5476 (2007). https://doi.org/10.1038/sj.onc.1210614

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