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

Molecular Biology

Journal of Cell Science & Therapy

Author(s): Boyault C, Sadoul K, Pabion M, Khochbin S

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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. This article was published in Oncogene and referenced in Journal of Cell Science & Therapy

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