The tubulin code: Molecular components, readout mechanisms, and functions

• Published in: The Journal of cell biology Vol. 206; no. 4; pp. 461 - 472
• Main Author: Janke, Carsten
• Format: Journal Article
• Language: English
• Published: United States Rockefeller University Press 18.08.2014; The Rockefeller University Press
• Subjects: Acetylation; Cells; Cytoskeleton; Eukaryota; Glutamic Acid - metabolism; Glycine - metabolism; Heterogeneity; Microtubule-Associated Proteins; Microtubules - metabolism; Molecules; Protein Isoforms; Protein Processing, Post-Translational - physiology; Proteins; Reviews; Tubulin - metabolism; Tyrosine - metabolism
• ISSN: 0021-9525; 1540-8140; 1540-8140
• DOI: 10.1083/jcb.201406055

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.