title: Hyperglutamylation of tubulin can either stabilize or destabilize microtubules in the same cell.
abstract: In most eukaryotic cells, tubulin is subjected to posttranslational glutamylation, a conserved modification of unclear function. The glutamyl side chains form as branches of the primary sequence glutamic acids in two biochemically distinct steps: initiation and elongation. The length of the glutamyl side chain is spatially controlled and microtubule type specific. Here, we probe the significance of the glutamyl side chain length regulation in vivo by overexpressing a potent side chain elongase enzyme, Ttll6Ap, in Tetrahymena. Overexpression of Ttll6Ap caused hyperelongation of glutamyl side chains on the tubulin of axonemal, cortical, and cytoplasmic microtubules. Strikingly, in the same cell, hyperelongation of glutamyl side chains stabilized cytoplasmic microtubules and destabilized axonemal microtubules. Our observations suggest that the cellular outcomes of glutamylation are mediated by spatially restricted tubulin interactors of diverse nature.
authors.affiliation: Department of Cellular Biology, University of Georgia, Athens, GA 30602-2607, USA.
authors.forename: Dorota
authors.initials: D
authors.lastname: Wloga
authors.forename: Drashti
authors.initials: D
authors.lastname: Dave
authors.forename: Jennifer
authors.initials: J
authors.lastname: Meagley
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Rogowski
authors.forename: Maria
authors.initials: M
authors.lastname: Jerka-Dziadosz
authors.forename: Jacek
authors.initials: J
authors.lastname: Gaertig
mesh_terms: D000818:Animals; D054468:Axoneme / Q000378:metabolism / Q000648:ultrastructure; D002923:Cilia / Q000378:metabolism / Q000648:ultrastructure; D018698:Glutamic Acid / Q000737:chemistry / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D016808:Tetrahymena thermophila / Q000166:cytology / Q000378:metabolism; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism*; D050257:Tubulin Modulators / Q000378:metabolism
chemical_list: D015800:Protozoan Proteins; D011993:Recombinant Fusion Proteins; D014404:Tubulin; D050257:Tubulin Modulators; D018698:Glutamic Acid
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