[On the road to deciphering the tubulin code: focus on acetylation and detyrosination].

Med Sci (Paris)

Régulation et pharmacologie du cytosquelette, Institut pour l'avancée des biosciences, Université Grenoble Alpes ; Inserm U 1209 ; CNRS 5309, Allée des Alpes, 38700 La Tronche, France.

Published: December 2018

AI Article Synopsis

  • Microtubules are made from α- and β-tubulin proteins and play key roles in cell shape, movement, and division.
  • They can change quickly or remain stable based on the cell’s needs.
  • This review highlights two important modifications of microtubules—acetylation and detyrosination of α-tubulin—and how their dysfunction is linked to various diseases.

Article Abstract

Microtubules are cytoskeletal fibers formed by the assembly of α- and β-tubulin heterodimers. They contribute to cell morphology, mobility and polarity, as well as to cellular transport processes and cell division. The microtubular network constantly adapts to cellular needs and may be composed of very dynamic or more stable microtubules. To regulate their diverse functions in a spatio-temporal manner, microtubules are subjected to numerous reversible post-translational modifications, which generate the "tubulin code". This review focuses on two modifications characteristic of stable microtubules - acetylation and detyrosination of α-tubulin - and their deregulation in certain pathologies.

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Source
http://dx.doi.org/10.1051/medsci/2018295DOI Listing

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