Tubulin code

Génétique, biologie cellulaire et développement

Microtubules (MTs) are essential cytoskeletal elements composed of alpha- and beta-Tubulin heterodimers. They are involved in a range of cellular functions including cell division, maintenance of cell shape, intracellular transport as well as cell motility.

The mechanisms that allow MTs to perform such a diverse range of functions are poorly understood, but it is clear that each specific MT function requires the recruitment of a particular set of MT-associated proteins (MAPs). Strikingly, many MAPs interact with the C-terminal tails of Tubulins, which are known to protrude from the MT surface and to undergo several unusual post-translational modifications (Westermann and Weber, 2003).

Such Tubulin C-terminal modifications include the removal of the very C-terminal tyrosine from alpha-Tubulin and two so-called poly-modifications, namely poly-glutamylation and poly-glycylation, which consist in the addition of side chains of either glutamate or glycine residues to the C-terminal tails of both alpha- and beta-Tubulin.

The combination of the different Tubulin C-terminal modifications together with the fact that the side chains generated by the poly-modifications vary in length provides a high potential for encoding patterns on the MT surface that might recruit specific MAPs and allow the functional adaptation of MTs.
In addition, since all these modifications have been shown to be reversible, they permit rapid changes in the MT properties.


Ghislain GILLARD

Francois JUGE

Krzysztof ROGOWSKI

Clémence Gaufichon

Samer Kiwan


Publications de l'équipe

A family of carboxypeptidases catalyzing α- and β-tubulin tail processing and deglutamylation.

Nicot S, Gillard G, Impheng H, Joachimiak E, Urbach S, Mochizuki K, Wloga D, Juge F, Rogowski K

A release-and-capture mechanism generates an essential non-centrosomal microtubule array during tube budding.

Gillard G, Girdler G, Röper K

Modulation of Yorkie activity by alternative splicing is required for developmental stability.

Srivastava D, de Toledo M, Manchon L, Tazi J, Juge F

Tubulin modifying enzymes as target for the treatment of tau-related diseases

Krzysztof Rogowski, Khaled Hached, Carole Crozet, Siem Van Der Laan

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Control of cell shape during epithelial morphogenesis: recent advances.

Gillard G, Röper K

Evolutionary Divergence of Enzymatic Mechanisms for Tubulin Detyrosination.

van der Laan S, Lévêque MF, Marcellin G, Vezenkov L, Lannay Y, Dubra G, Bompard G, Ovejero S, Urbach S, Burgess A, Amblard M, Sterkers Y, Bastien P, Rogowski K

Tubulin glutamylation: a skeleton key for neurodegenerative diseases.

van der Laan S, Dubra G, Rogowski K

Force Transmission between Three Tissues Controls Bipolar Planar Polarity Establishment and Morphogenesis.

Gillard G, Nicolle O, Brugière T, Prigent S, Pinot M, Michaux G

CSAP acts as a regulator of TTLL-mediated microtubule glutamylation

Bompard G, van Dijk J, Cau J, Marcellin G, Lannay Y, Lawera A, van der Laan S and Rogowski K.

+ Plateau d'Imagerie Cellulaire

Microtubule polyglutamylation and acetylation drive microtubule dynamics critical for platelet formation.

van Dijk J, Bompard G, Cau J, Kunishima S, Rabeharivelo G, Mateos-Langerak J, Cazevieille C, Cavelier P, Boizet-Bonhoure B, Delsert C, Morin N

+ Développement et Pathologie de la Gonade

Vasohibins/SVBP are tubulin carboxypeptidases (TCP) that regulate neuron differentiation

Aillaud, C., Bosc, C., Peris, L., Bosson, A., Heemeryck, P.,Van Dijk, J., Le Friec, J., Boulan, B., Vossier, F., Sanman, L.E., Syed, S., Amara, N., Couté, Y., Lafanechère, L., Denarier, E., Delphin, C., Pelletier, L., Humbert, S., Bogyo, M., Andrieux*, A., Rogowski*, K., Moutin*, M.J.

Identification of DmTTLL5 as a Major Tubulin Glutamylase in the Drosophila Nervous System

Devambez I, van Dijk J, Benlefki S, Layalle S, Grau Y, Rogowski K, Parmentier ML, Soustelle L.

Novel interactors of the Drosophila Survival Motor Neuron (SMN) Complex suggest its full conservation.

Lanfranco M, Cacciottolo R, Borg RM, Vassallo N, Juge F, Bordonné R, Cauchi RJ

Splicing factors act as genetic modulators of TDP-43 production in a new autoregulatory TDP-43 Drosophila model.

Pons M, Miguel L, Miel C, Avequin T, Juge F, Frebourg T, Campion D, Lecourtois M

Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells.

Gillard G, Shafaq-Zadah M, Nicolle O, Damaj R, Pécréaux J, Michaux G

A role for the serine/arginine-rich (SR) protein B52/SRSF6 in cell growth and myc expression in Drosophila.

Fernando C, Audibert A, Simon F, Tazi J, Juge F

Multifunctional RNA processing protein SRm160 induces apoptosis and regulates eye and genital development in Drosophila.

Fan YJ, Gittis AH, Juge F, Qiu C, Xu YZ, Rabinow L

Regulated functional alternative splicing in Drosophila.

Venables JP, Tazi J, Juge F

A family of protein-deglutamylating enzymes associated with neurodegeneration.

Rogowski K, van Dijk J, Magiera MM, Bosc C, Deloulme JC, Bosson A, Peris L, Gold ND, Lacroix B, Bosch Grau M, Bec N, Larroque C, Desagher S, Holzer M, Andrieux A, Moutin MJ, Janke C

The SR protein B52/SRp55 is required for DNA topoisomerase I recruitment to chromatin, mRNA release and transcription shutdown.

Juge F, Fernando C, Fic W, Tazi J

Tubulin polyglutamylation stimulates spastin-mediated microtubule severing.

Lacroix B, van Dijk J, Gold ND, Guizetti J, Aldrian-Herrada G, Rogowski K, Gerlich DW, Janke C

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

Wloga D, Dave D, Meagley J, Rogowski K, Jerka-Dziadosz M, Gaertig J

TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia.

Wloga D, Webster DM, Rogowski K, Bré MH, Levilliers N, Jerka-Dziadosz M, Janke C, Dougan ST, Gaertig J

Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.

Rogowski K, Juge F, van Dijk J, Wloga D, Strub JM, Levilliers N, Thomas D, Bré MH, Van Dorsselaer A, Gaertig J, Janke C

Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila.

Wloga D, Rogowski K, Sharma N, Van Dijk J, Janke C, Eddé B, Bré MH, Levilliers N, Redeker V, Duan J, Gorovsky MA, Jerka-Dziadosz M, Gaertig J

Polyglutamylation: a fine-regulator of protein function? 'Protein Modifications: beyond the usual suspects' review series.

Janke C, Rogowski K, van Dijk J

A targeted multienzyme mechanism for selective microtubule polyglutamylation.

van Dijk J, Rogowski K, Miro J, Lacroix B, Eddé B, Janke C

Eye development under the control of SRp55/B52-mediated alternative splicing of eyeless.

Fic W, Juge F, Soret J, Tazi J

Tubulin polyglutamylase enzymes are members of the TTL domain protein family.

Janke C, Rogowski K, Wloga D, Regnard C, Kajava AV, Strub JM, Temurak N, van Dijk J, Boucher D, van Dorsselaer A, Suryavanshi S, Gaertig J, Eddé B