期刊
DEVELOPMENTAL CELL
卷 16, 期 6, 页码 867-876出版社
CELL PRESS
DOI: 10.1016/j.devcel.2009.04.008
关键词
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资金
- National Science Foundation [MBC-033965]
- American Cancer Society [DDC-112979]
- Association de la Recherche contre le Cancer [CR504/7817, 3140]
- French National Research Agency [JC0542022]
- EMBO long-term fellowships [JG/VP-5454, ALTF 546-2006]
In most ciliated cell types, tubulin is modified by glycylation, a posttranslational modification of unknown function. We show that the TTLL3 proteins act as tubulin glycine ligases with chain-initiating activity. In Tetrahymena, deletion of TTLL3 shortened axonemes and increased their resistance to paclitaxel-mediated microtubule stabilization. In zebrafish, depletion of TTLL3 led to either shortening or loss of cilia in several organs, including the Kupffer's vesicle and olfactory placode. We also show that, in vivo, glutamic acid and glycine ligases oppose each other, likely by competing for shared modification sites on tubulin. We propose that tubulin glycylation regulates the assembly and dynamics of axonemal microtubules and acts either directly or indirectly by inhibiting tubulin glutamylation.
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