Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Bernard Eddé"'
Autor:
Dorota Wloga, Bernard Eddé, Juliette van Dijk, Virginie Redeker, Krzysztof Rogowski, Maria Jerka-Dziadosz, Marie-Hélène Bré, Martin A. Gorovsky, Jacek Gaertig, Jianming Duan, Carsten Janke, Neeraj Sharma, Nicolette Levilliers
Publikováno v:
Eukaryotic Cell
Eukaryotic Cell, American Society for Microbiology, 2008, 7 (8), pp.1362-72. ⟨10.1128/EC.00084-08⟩
Eukaryotic Cell, American Society for Microbiology, 2008, 7 (8), pp.1362-72. ⟨10.1128/EC.00084-08⟩
Tubulin undergoes glutamylation, a conserved posttranslational modification of poorly understood function. We show here that in the ciliate Tetrahymena , most of the microtubule arrays contain glutamylated tubulin. However, the length of the polyglut
Autor:
Alain Van Dorsselaer, Jean-Marc Strub, Juliette van Dijk, Bernard Eddé, Julie Miro, Benjamin Lacroix, Carsten Janke
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 283 (7), pp.3915-3922. ⟨10.1074/jbc.M705813200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 283 (7), pp.3915-3922. ⟨10.1074/jbc.M705813200⟩
Polyglutamylation is a post-translational modification that generates lateral acidic side chains on proteins by sequential addition of glutamate amino acids. This modification was first discovered on tubulins, and it is important for several microtub
Autor:
Bernard Eddé, Julie Miro, Krzysztof Rogowski, Juliette van Dijk, Benjamin Lacroix, Carsten Janke
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2007, 26 (3), pp.437-48. ⟨10.1016/j.molcel.2007.04.012⟩
Molecular Cell, Elsevier, 2007, 26 (3), pp.437-48. ⟨10.1016/j.molcel.2007.04.012⟩
Polyglutamylases are enzymes that form polyglutamate side chains of variable lengths on proteins. Polyglutamylation of tubulin is believed to regulate interactions of microtubules (MTs) with MT-associated proteins and molecular motors. Subpopulations
Publikováno v:
Journal of Cell Science. 112:4281-4289
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
Autor:
Daniel White, Bernard Eddé, Claude Gagnon, Jacky Cosson, Philippe Huitorel, Stéphane Audebert
Publikováno v:
European Journal of Biochemistry. 261:48-56
Flagellar motility is the result of specific interactions between axonemal microtubular proteins and the dynein motors. Tubulin, the main component of microtubule, is a very polymorphic protein resulting from the expression of several isogenes and fr
Publikováno v:
The Journal of Cell Biology
Glutamylation is the major posttranslational modification of neuronal and axonemal tubulin and is restricted predominantly to centrioles in nonneuronal cells (Bobinnec, Y., M. Moudjou, J.P. Fouquet, E. Desbruyères, B. Eddé, and M. Bornens. 1998. Ce
Publikováno v:
Biochemistry. 37:8395-8404
In this work, we report on a novel enzyme, tubulin polyglutamylase, which catalyzes the posttranslational formation of polyglutamyl side chains onto alpha- and beta-tubulin. The length of the polyglutamyl side chain regulates the interaction between
Publikováno v:
Cell Motility and the Cytoskeleton. 39:223-232
We have examined the distribution of glutamylated tubulin in non-neuronal cell lines. A major part of centriole tubulin is highly modified on both the alpha- and beta-tubulin subunits, whereas a minor part of the cytoplasmic tubulin is slightly modif
Autor:
E Desbruyeres, C Gruszczynski, François Gros, Bernard Eddé, Stéphane Audebert, Philippe Denoulet, Annette Koulakoff
Publikováno v:
Molecular Biology of the Cell. 4:615-626
The relationship between microtubule dynamics and polyglutamylation of tubulin was investigated in young differentiating mouse brain neurons. Selective posttranslational labeling with [3H]glutamate and immunoblotting with a specific monoclonal antibo
Autor:
Jean-Claude Promé, Bernard Eddé, François Gros, E Desbruyeres, Jean Pierre Le Caer, Philippe Denoulet, Jean Rossier
Publikováno v:
Biochemistry. 31:403-410
We have previously identified a major modification of neuronal alpha-tubulin which consists of the posttranslational addition of a varying number of glutamyl units on the gamma-carboxyl group of glutamate residue 445. This modification, called polygl