Research Articles

Tubulin Polyglutamylase Enzymes Are Members of the TTL Domain Protein Family

Carsten Janke,^1* Krzysztof Rogowski,^2* Dorota Wloga,^2* Catherine Regnard,³ Andrey V. Kajava,¹ Jean-Marc Strub,⁴ Nevzat Temurak,¹ Juliette van Dijk,¹ Dominique Boucher,⁵ Alain van Dorsselaer,⁴ Swati Suryavanshi,² Jacek Gaertig,² Bernard Eddé^1,6

Polyglutamylation of tubulin has been implicated in several functions of microtubules, but the identification of the responsible enzyme(s) has been challenging. We found that the neuronal tubulin polyglutamylase is a protein complex containing a tubulin tyrosine ligase–like (TTLL) protein, TTLL1. TTLL1 is a member of a large family of proteins with a TTL homology domain, whose members could catalyze ligations of diverse amino acids to tubulins or other substrates. In the model protist Tetrahymena thermophila, two conserved types of polyglutamylases were characterized that differ in substrate preference and subcellular localization.

¹ Centre de Recherches de Biochimie Macromoléculaire, CNRS, 34293 Montpellier, France.
² Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA.
³ Department of Molecular Biology, Adolf Butenandt Institute, 80336 Munich, Germany.
⁴ Université Louis Pasteur, 67087 Strasbourg, France.
⁵ Laboratoire de Biochimie Cellulaire, CNRS, Université Paris 6, 75252 Paris, France.
⁶ Université Paris 6, 75252 Paris, France.

^* These authors contributed equally to this work.

To whom correspondence should be addressed. E-mail: jgaertig{at}cb.uga.edu; bernard.edde{at}crbm.cnrs.fr

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The Caenorhabditis elegans nephrocystins act as global modifiers of cilium structure.

A. R. Jauregui, K. C.Q. Nguyen, D. H. Hall, and M. M. Barr (2008)
J. Cell Biol. 180, 973-988
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Polyglutamylation Is a Post-translational Modification with a Broad Range of Substrates.

J. van Dijk, J. Miro, J.-M. Strub, B. Lacroix, A. van Dorsselaer, B. Edde, and C. Janke (2008)
J. Biol. Chem. 283, 3915-3922
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The Zebrafish fleer Gene Encodes an Essential Regulator of Cilia Tubulin Polyglutamylation.

N. Pathak, T. Obara, S. Mangos, Y. Liu, and I. A. Drummond (2007)
Mol. Biol. Cell 18, 4353-4364
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Katanin regulates dynamics of microtubules and biogenesis of motile cilia.

N. Sharma, J. Bryant, D. Wloga, R. Donaldson, R. C. Davis, M. Jerka-Dziadosz, and J. Gaertig (2007)
J. Cell Biol. 178, 1065-1079
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Endoplasmic Reticulum Retention Signal-Dependent Glycylation of the Hsp70/Grp170-Related Pgp1p in Tetrahymena.

R. Xie, K. M. Clark, and M. A. Gorovsky (2007)
Eukaryot. Cell 6, 388-397
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A novel subfamily of mouse cytosolic carboxypeptidases.

E. Kalinina, R. Biswas, I. Berezniuk, A. Hermoso, F. X. Aviles, and L. D. Fricker (2007)
FASEB J 21, 836-850
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Loss of {alpha}-tubulin polyglutamylation in ROSA22 mice is associated with abnormal targeting of KIF1A and modulated synaptic function.

K. Ikegami, R. L. Heier, M. Taruishi, H. Takagi, M. Mukai, S. Shimma, S. Taira, K. Hatanaka, N. Morone, I. Yao, et al. (2007)
PNAS 104, 3213-3218
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TTLL7 Is a Mammalian beta-Tubulin Polyglutamylase Required for Growth of MAP2-positive Neurites.

K. Ikegami, M. Mukai, J.-i. Tsuchida, R. L. Heier, G. R. MacGregor, and M. Setou (2006)
J. Biol. Chem. 281, 30707-30716
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Tetrahymena Genome Database (TGD): a new genomic resource for Tetrahymena thermophila research.

N. A. Stover, C. J. Krieger, G. Binkley, Q. Dong, D. G. Fisk, R. Nash, A. Sethuraman, S. Weng, and J. M. Cherry (2006)
Nucleic Acids Res. 34, D500-D503
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