title: The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions.
abstract: Cellular microtubules are marked by abundant and evolutionarily conserved post-translational modifications that have the potential to tune their functions. This review focuses on the astonishing chemical complexity introduced in the tubulin heterodimer at the post-translational level and summarizes the recent advances in identifying the enzymes responsible for these modifications and deciphering the consequences of tubulin's chemical diversity on the function of molecular motors and microtubule associated proteins.
authors.affiliation: Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland, USA.
authors.forename: Christopher P
authors.initials: CP
authors.lastname: Garnham
authors.forename: Antonina
authors.initials: A
authors.lastname: Roll-Mecak
mesh_terms: D000107:Acetylation; D000818:Animals; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D011499:Protein Processing, Post-Translational; D014404:Tubulin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D008869:Microtubule-Associated Proteins; D014404:Tubulin