Literature DB >> 20940043

The ins and outs of tubulin acetylation: more than just a post-translational modification?

Daniel Perdiz1, Rafah Mackeh, Christian Poüs, Anita Baillet.   

Abstract

Microtubules are highly dynamic polymers of α/β tubulin heterodimers that play key roles in cell division and in organizing cell cytoplasm. Although they have been discovered more than two decades ago, tubulin post-translational modifications recently gained a new interest as their role was increasingly highlighted in neuron differentiation and neurodegenerative disorders. Here, we specifically focus on tubulin acetylation from its discovery to recent studies that provide new insights into how it is regulated in health and disease and how it impacts microtubule functions. Even though new mechanisms involving tubulin acetylation are regularly being uncovered, the molecular links between its location inside the microtubule lumen and its regulators and effectors is still poorly understood. This review highlights the emerging roles of tubulin acetylation in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signalling. It also points out that tubulin acetylation should no longer be seen as a passive marker of microtubule stability, but as a broad regulator of microtubule functions.
Copyright © 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20940043     DOI: 10.1016/j.cellsig.2010.10.014

Source DB:  PubMed          Journal:  Cell Signal        ISSN: 0898-6568            Impact factor:   4.315


  95 in total

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Journal:  ACS Chem Neurosci       Date:  2018-12-14       Impact factor: 4.418

2.  The microtubule cytoskeleton is required for a G2 cell cycle delay in cancer cells lacking stathmin and p53.

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Journal:  Cytoskeleton (Hoboken)       Date:  2012-03-29

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Authors:  Elena Kypri; Andri Christodoulou; Giannis Maimaris; Mette Lethan; Maria Markaki; Costas Lysandrou; Carsten W Lederer; Nektarios Tavernarakis; Stefan Geimer; Lotte B Pedersen; Niovi Santama
Journal:  Cell Mol Life Sci       Date:  2013-06-27       Impact factor: 9.261

4.  The focal adhesion protein kindlin-2 controls mitotic spindle assembly by inhibiting histone deacetylase 6 and maintaining α-tubulin acetylation.

Authors:  Hui-Foon Tan; Suet-Mien Tan
Journal:  J Biol Chem       Date:  2020-03-13       Impact factor: 5.157

Review 5.  Cardiac microtubules in health and heart disease.

Authors:  Matthew A Caporizzo; Christina Yingxian Chen; Benjamin L Prosser
Journal:  Exp Biol Med (Maywood)       Date:  2019-08-09

Review 6.  Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development.

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Journal:  Signal Transduct Target Ther       Date:  2020-07-13

7.  αTAT1 catalyses microtubule acetylation at clathrin-coated pits.

Authors:  Guillaume Montagnac; Vannary Meas-Yedid; Marie Irondelle; Antonio Castro-Castro; Michel Franco; Toshinobu Shida; Maxence V Nachury; Alexandre Benmerah; Jean-Christophe Olivo-Marin; Philippe Chavrier
Journal:  Nature       Date:  2013-10-06       Impact factor: 49.962

8.  Pro-autophagic polyphenols reduce the acetylation of cytoplasmic proteins.

Authors:  Federico Pietrocola; Guillermo Mariño; Delphine Lissa; Erika Vacchelli; Shoaib Ahmad Malik; Mireia Niso-Santano; Naoufal Zamzami; Lorenzo Galluzzi; Maria Chiara Maiuri; Guido Kroemer
Journal:  Cell Cycle       Date:  2012-10-15       Impact factor: 4.534

9.  Demonstration of primary cilia and acetylated α-tubulin in fish endothelial, epithelial and fibroblast cell lines.

Authors:  Nguyen T K Vo; Niels C Bols
Journal:  Fish Physiol Biochem       Date:  2015-08-07       Impact factor: 2.794

10.  Lysine acetyltransfer supports platelet function.

Authors:  J E Aslan; R A Rigg; M S Nowak; C P Loren; S M Baker-Groberg; J Pang; L L David; O J T McCarty
Journal:  J Thromb Haemost       Date:  2015-08-29       Impact factor: 5.824

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