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Oncogene. 2007 Aug 13;26(37):5468-76.

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

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


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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