Carboxyterminal post-translational modifications of tubulin

Stable Identifier
Homo sapiens
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Tubulins fold into compact globular domains with less structured carboxyterminal tails. These tails vary in sequence between tubulin isoforms and are exposed on the surfaces of microtubules. They can undergo a variety of posttranslational modifications, including the attachment and removal of polyglutamate chains and in the case of alpha-tunulins the loss and reattachment of a terminal tyrosine (Tyr) residue. These modifications are associated with changes in the rigidity and stability of microtubules (Song & Brady 2015; Yu et al. 2015).
Mutations affecting these modification processes can have severe effects on phenotype (e.g., Ikegami et al. 2007). Nevertheless, the precise molecular mechanisms by which these changes in tubulin structure modulate its functions remain unclear, so these modification processes are simply annotated here as a series of chemical transformations of tubulins.
Literature References
PubMed ID Title Journal Year
25957412 Writing and Reading the Tubulin Code

Roll-Mecak, A, Yu, I, Garnham, CP

J. Biol. Chem. 2015
25468068 Post-translational modifications of tubulin: pathways to functional diversity of microtubules

Brady, ST, Song, Y

Trends Cell Biol. 2015
17360631 Loss of alpha-tubulin polyglutamylation in ROSA22 mice is associated with abnormal targeting of KIF1A and modulated synaptic function

Mukai, M, Takagi, H, Setou, M, Hatanaka, K, Campbell, PK, Ikegami, K, Yao, I, Morone, N, Shimma, S, Taira, S, Taruishi, M, Macgregor, GR, Heier, RL, Yuasa, S, Janke, C

Proc. Natl. Acad. Sci. U.S.A. 2007
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Orthologous Events
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