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Vol. 15, Issue 9, 4136-4147, September 2004

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Cell Context-specific Effects of the -Tubulin Glycylation Domain on Assembly and Size of Microtubular Organelles

Rupal Thazhath ^*, Maria Jerka-Dziadosz , Jianming Duan  , Dorota Wloga ^*, Martin A. Gorovsky , Joseph Frankel ^||, and Jacek Gaertig ^* ¶

^* Department of Cellular Biology, University of Georgia, Athens, GA 30602; Department of Cell Biology, M. Nencki Institute of Experimental Biology, Polish Academy of Science, 02-093 Warsaw, Poland; Department of Biology, University of Rochester, Rochester, NY 14627; and ^|| Department of Biological Sciences, University of Iowa, Iowa City, IA 52242

Submitted March 23, 2004; Revised May 26, 2004; Accepted June 29, 2004
Monitoring Editor: J. Richard McIntosh

Tubulin glycylation is a posttranslational modification found in cells with cilia or flagella. The ciliate Tetrahymena has glycylation on ciliary and cortical microtubules. We showed previously that mutating three glycylation sites on -tubulin produces immotile 9 + 0 axonemes and inhibits cytokinesis. Here, we use an inducible glycylation domain mutation and epitope tagging to evaluate the potential of glycylation-deficient tubulin for assembly and maintenance of microtubular systems. In axonemes, the major defects, including lack of the central pair, occurred during assembly, and newly made cilia were abnormally short. The glycylation domain also was required for maintenance of the length of already assembled cilia. In contrast to the aberrant assembly of cilia, several types of cortical organelles showed an abnormally high number of microtubules in the same mutant cells. Thus, the consequences of deficiency in tubulin glycylation are organelle type specific and lead to either insufficient assembly (cilia) or excessive assembly (basal bodies and cortical microtubules). We suggest that the diverse functions of the -tubulin glycylation domain are executed by spatially restricted microtubule-associated proteins.

Abbreviations used: AZM, adoral zone of membranelles; BB, basal body; Cd, cadmium; CP, central pair; CVP, contractile vacuole pore; HA hemagglutinin; IFT, intraflagellar transport; LM, longitudinal microtubule; MAP, microtubule-associated protein; MT, microtubule; PC, postciliary microtubule; pm, paromomycin; TuG, tubulin glycylation; TM, transverse microtubule; UM, undulating membrane; WT, wild-type.

Present address: Head and Neck Surgery Branch, NIDCD, National Institutes of Health, Bethesda, MD 20892.

^¶ Corresponding author. E-mail address: jgaertig{at}cb.uga.edu.

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