title: The tubulin code: molecular components, readout mechanisms, and functions.
abstract: Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a "tubulin code" that coordinates the complex functions of microtubules in cells.
authors.affiliation: Institut Curie, 91405 Orsay, France Centre National de la Recherche Scientifique Unité Mixte de Recherche 3306, 91405 Orsay, France Institut National de la Santé et de la Recherche Médicale U1005, 91405 Orsay, France Paris Sciences et Lettres Research University, 75005 Paris, France Carsten.Janke@curie.fr.
authors.forename: Carsten
authors.initials: C
authors.lastname: Janke
mesh_terms: D000107:Acetylation; D056890:Eukaryota; D018698:Glutamic Acid / Q000378:metabolism; D005998:Glycine / Q000378:metabolism; D008869:Microtubule-Associated Proteins; D008870:Microtubules / Q000378:metabolism*; D020033:Protein Isoforms; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D014404:Tubulin / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism
chemical_list: D008869:Microtubule-Associated Proteins; D020033:Protein Isoforms; D014404:Tubulin; D018698:Glutamic Acid; D014443:Tyrosine; D005998:Glycine