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Cell Mol Life Sci. 2015 Nov;72(22):4237-55. doi: 10.1007/s00018-015-2000-5. Epub 2015 Jul 31.

Tubulin acetylation: responsible enzymes, biological functions and human diseases.

Li L1,2, Yang XJ3,4,5,6.

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Rosalind and Morris Goodman Cancer Research Center, Montreal, QC, H3A 1A3, Canada.
Department of Medicine, Montreal, QC, H3A 1A3, Canada.
Rosalind and Morris Goodman Cancer Research Center, Montreal, QC, H3A 1A3, Canada.
Department of Medicine, Montreal, QC, H3A 1A3, Canada.
Department of Biochemistry, McGill University, Montreal, QC, H3A 1A3, Canada.
McGill University Health Center, Montreal, QC, H3A 1A3, Canada.


Microtubules have important functions ranging from maintenance of cell morphology to subcellular transport, cellular signaling, cell migration, and formation of cell polarity. At the organismal level, microtubules are crucial for various biological processes, such as viral entry, inflammation, immunity, learning and memory in mammals. Microtubules are subject to various covalent modifications. One such modification is tubulin acetylation, which is associated with stable microtubules and conserved from protists to humans. In the past three decades, this reversible modification has been studied extensively. In mammals, its level is mainly governed by opposing actions of α-tubulin acetyltransferase 1 (ATAT1) and histone deacetylase 6 (HDAC6). Knockout studies of the mouse enzymes have yielded new insights into biological functions of tubulin acetylation. Abnormal levels of this modification are linked to neurological disorders, cancer, heart diseases and other pathological conditions, thereby yielding important therapeutic implications. This review summarizes related studies and concludes that tubulin acetylation is important for regulating microtubule architecture and maintaining microtubule integrity. Together with detyrosination, glutamylation and other modifications, tubulin acetylation may form a unique 'language' to regulate microtubule structure and function.


Axon regeneration; HDAC inhibitor; HDAC5; Inflammation; Lysine acetylation; Mec17; Mechanosensing; Pillar cell; SIRT2; Touch receptor neuron; Tubulin code

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