Reactome | Carboxyterminal post-translational modifications of tubulin

Carboxyterminal post-translational modifications of tubulin

Stable Identifier

R-HSA-8955332

Type

Pathway

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Carboxyterminal post-translational modifications of tubulin

Click the image above or here to open this pathway in the Pathway Browser

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