Mutations of Tubulin Glycylation Sites Reveal Cross-talk between the C Termini of α- and β-Tubulin and Affect the Ciliary Matrix in Tetrahymena-Reference-Cited by-同舟云学术

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Mutations of Tubulin Glycylation Sites Reveal Cross-talk between the C Termini of α- and β-Tubulin and Affect the Ciliary Matrix in Tetrahymena

Published:2005-01 Issue:1 Volume:280 Page:596-606
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Redeker Virginie,Levilliers Nicolette,Vinolo Emilie,Rossier Jean,Jaillard Danielle,Burnette Dylan,Gaertig Jacek,Bré Marie-Hélène

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference83 articles.

1. Tubulin Post-Translational Modifications. Enzymes and Their Mechanisms of Action

2. Multiple Forms of Tubulin: Different Gene Products and Covalent Modifications

3. Cytoskeleton: Functions for tubulin modifications at last

4. Post-translational modifications regulate microtubule function

5. Posttranslational Glutamylation of α-tubulin

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1. Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins;Molecular Biology of the Cell;2024-07-01

2. Structural basis for α-tubulin-specific and modification state-dependent glutamylation;Nature Chemical Biology;2024-04-24

3. Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii;Microorganisms;2024-02-28

4. The Tubulin Code, from Molecules to Health and Disease;Annual Review of Cell and Developmental Biology;2023-10-16

5. α- and β-tubulin C-terminal tails with distinct modifications are crucial for ciliary motility and assembly;Journal of Cell Science;2023-08-15

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