caa a22 4500 606175652 CHVBK 20210128100744.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00018-015-2000-5 doi (NATIONALLICENCE)springer-10.1007/s00018-015-2000-5 Tubulin acetylation: responsible enzymes, biological functions and human diseases [Elektronische Daten] [Lin Li, Xiang-Jiao Yang] 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. Springer Basel, 2015 Tubulin code nationallicence Lysine acetylation nationallicence Mec17 nationallicence HDAC5 nationallicence SIRT2 nationallicence Mechanosensing nationallicence Touch receptor neuron nationallicence Pillar cell nationallicence Axon regeneration nationallicence Inflammation nationallicence HDAC inhibitor nationallicence Li Lin Rosalind and Morris Goodman Cancer Research Center, H3A 1A3, Montreal, QC, Canada aut Yang Xiang-Jiao Rosalind and Morris Goodman Cancer Research Center, H3A 1A3, Montreal, QC, Canada aut Cellular and Molecular Life Sciences Springer Basel 72/22(2015-11-01), 4237-4255 1420-682X 72:22<4237 2015 72 18 https://doi.org/10.1007/s00018-015-2000-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-2000-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Li Lin Rosalind and Morris Goodman Cancer Research Center, H3A 1A3, Montreal, QC, Canada aut NATIONALLICENCE 700 1- Yang Xiang-Jiao Rosalind and Morris Goodman Cancer Research Center, H3A 1A3, Montreal, QC, Canada aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/22(2015-11-01), 4237-4255 1420-682X 72:22<4237 2015 72 18