EC Accepts, published online ahead of print on 21 August 2009

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Eukaryotic Cell doi:10.1128/EC.00176-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Hyperglutamylation of tubulin can either stabilize or destabilize microtubules in the same cell.

Dorota Wloga, Drashti Dave, Jennifer Meagley, Krzysztof Rogowski, Maria Jerka-Dziadosz, and Jacek Gaertig^*

Department of Cellular Biology, University of Georgia, Athens GA 30602-2607; Department of Cell Biology, M. Nencki Institute of Experimental Biology, Polish Academy of Science, 02-093 Warsaw, Poland

^* To whom correspondence should be addressed. Email: jgaertig{at}cb.uga.edu.

In most eukaryotic cells, tubulin is subjected to post-translational 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 hyper-elongation of glutamyl side chains on tubulin of axonemal, cortical and cytoplasmic microtubules. Strikingly, in the same cell, hyper-elongation of glutamyl side chains stabilized cytoplasmic, and destabilized axonemal microtubules, respectively. Our observations suggest that the cellular outcomes of glutamylation are mediated by spatially-restricted tubulin interactors of diverse nature.