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Journal of Cell Science, Vol 112, Issue 23 4281-4289, Copyright © 1999 by Company of Biologists
JOURNAL ARTICLES |
C Regnard, E Desbruyeres, P Denoulet and B Edde
Laboratoire de Biochimie Cellulaire, CNRS UPR 9065 and Universite Paris VI, College de France, 75005 Paris. regnard@ext.jussieu.fr
Polyglutamylation is a posttranslational modification of tubulin that is very common in neurons and ciliated or flagellated cells. It was proposed to regulate the binding of microtubule associated proteins (MAPs) and molecular motors as a function of the length of the polyglutamyl side-chain. Though much less common, this modification of tubulin also occurs in proliferating cells like HeLa cells where it is associated with centrioles and with the mitotic spindle. Recently, we partially purified tubulin polyglutamylase from mouse brain and described its enzymatic properties. In this work, we focused on tubulin polyglutamylase activity from HeLa cells. Our results support the existence of a tubulin polyglutamylase family composed of several isozymic variants specific for alpha- or beta-tubulin subunits. In the latter case, the specificity probably also concerns the different beta-tubulin isotypes. Interestingly, we found that tubulin polyglutamylase activity is regulated in a cell cycle dependent manner and peaks in G(2)-phase while the level of glutamylated tubulin peaks in mitosis. Consistent results were obtained by treating the cells with hydroxyurea, nocodazole or taxotere. In particular, in mitotic cells, tubulin polyglutamylase activity was always low while glutamylation level was high. Finally, tubulin polyglutamylase activity and the level of glutamylated tubulin appeared to be inversely related. This paradox suggests a complex regulation of both tubulin polyglutamylase and the reverse deglutamylase activity.
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 C. Janke, K. Rogowski, D. Wloga, C. Regnard, A. V. Kajava, J.-M. Strub, N. Temurak, J. van Dijk, D. Boucher, A. van Dorsselaer, et al. Tubulin Polyglutamylase Enzymes Are Members of the TTL Domain Protein Family Science, June 17, 2005; 308(5729): 1758 - 1762. [Abstract] [Full Text] [PDF]
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 C. Regnard, D. Fesquet, C. Janke, D. Boucher, E. Desbruyeres, A. Koulakoff, C. Insina, P. Travo, and B. Edde Characterisation of PGs1, a subunit of a protein complex co-purifying with tubulin polyglutamylase J. Cell Sci., October 15, 2003; 116(20): 4181 - 4190. [Abstract] [Full Text] [PDF]
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S. Westermann and K. Weber Identification of CfNek, a novel member of the NIMA family of cell cycle regulators, as a polypeptide copurifying with tubulin polyglutamylation activity in Crithidia J. Cell Sci., March 14, 2003; 115(24): 5003 - 5012. [Abstract] [Full Text] [PDF]
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C. Bonnet, D. Boucher, S. Lazereg, B. Pedrotti, K. Islam, P. Denoulet, and J. C. Larcher Differential Binding Regulation of Microtubule-associated Proteins MAP1A, MAP1B, and MAP2 by Tubulin Polyglutamylation J. Biol. Chem., April 13, 2001; 276(16): 12839 - 12848. [Abstract] [Full Text] [PDF]
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