skip to main content
Language:
Search Limited to: Search Limited to: Resource type Show Results with: Show Results with: Search type Index

Causes and Consequences of Microtubule Acetylation

Current biology, 2017-12, Vol.27 (23), p.R1287-R1292 [Peer Reviewed Journal]

2017 Elsevier Ltd ;Copyright © 2017 Elsevier Ltd. All rights reserved. ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0960-9822 ;EISSN: 1879-0445 ;DOI: 10.1016/j.cub.2017.10.044 ;PMID: 29207274

Full text available

Citations Cited by
  • Title:
    Causes and Consequences of Microtubule Acetylation
  • Author: Janke, Carsten ; Montagnac, Guillaume
  • Subjects: Acetylation ; Biochemistry ; Biochemistry, Molecular Biology ; Biomechanical Phenomena ; Biophysics ; Cell Behavior ; Cellular Biology ; Life Sciences ; Microtubules - metabolism ; Protein Processing, Post-Translational ; Stress, Mechanical ; Subcellular Processes
  • Is Part Of: Current biology, 2017-12, Vol.27 (23), p.R1287-R1292
  • Description: Among the different types of cytoskeletal components, microtubules arguably accumulate the greatest diversity of post-translational modifications (PTMs). Acetylation of lysine 40 (K40) of α-tubulin has received particular attention because it is the only tubulin PTM to be found in the lumen of microtubules: most other tubulin PTMs are found at the outer surface of the microtubule. As a consequence, the enzyme catalyzing K40 acetylation needs to penetrate the narrow microtubule lumen to find its substrate. Acetylated microtubules have been considered to be stable, long-lived microtubules; however, until recently, there was little information about whether the longevity of these microtubules is the cause or the consequence of acetylation. Current advances suggest that this PTM helps the microtubule lattice to cope with mechanical stress, thus facilitating microtubule self-repair. These observations now shed new light on the structural integrity of microtubules, as well as on the mechanisms and biological functions of tubulin acetylation. Here, we discuss recent insights into how acetylation is generated in the lumen of microtubules, and how this ‘hidden’ PTM can control the properties and functions of microtubules. In this Review, Janke and Montagnac discuss recent insights into the mechanisms responsible for acetylation in the lumen of microtubules and the effects of this luminal post-translational modification on the properties and functions of microtubules.
  • Publisher: England: Elsevier Ltd
  • Language: English
  • Identifier: ISSN: 0960-9822
    EISSN: 1879-0445
    DOI: 10.1016/j.cub.2017.10.044
    PMID: 29207274
  • Source: Cell Press Free Archives
    Hyper Article en Ligne (HAL) (Open Access)
    MEDLINE
Back to results list
Go to Previous pagePrevious Result  6 NextGo to Next page
INSPIRE LIBRARY - TON DUC THANG UNIVERSITY (84-028) 37 755 057 Feedback
19 Nguyen Huu Tho St. Dist.7, HCM thuvien@tdtu.edu.vn

Copyright © 2017 INSPIRE LIBRARY - TON DUC THANG UNIVERSITY

Searching Remote Databases, Please Wait