TTLL3, TTLL8, TTLL10 polyglycylate tubulin

Stable Identifier
R-HSA-8867370
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Tubulin is modified by glutamylation and glycylation, the additon of peptide branches made of glutamyl or glycyl residues respectively, which are attached to the gamma-carboxyl group of glutamic acids within the C-terminal tail domains of alpha- and beta-tubulin. They are added by members of the tubulin tyrosine ligase (TTL family). TTLL3, 8, and 10 are glycylases (Ikegami et al. 2008, Ikegami and Setou, 2009; Rogowski et al. 2009; Wloga et al. 2009) with TTLL3 and 8 serving as initiases, and TTLL10 serving as an elongase. In this event polyglycation is arbitrarily shown on only one tubulin protofilament within the microtubule.

Literature References
PubMed ID Title Journal Year
19524510 Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation

Rogowski, K, Juge, F, van Dijk, J, Wloga, D, Strub, JM, Levilliers, N, Thomas, D, Bré, MH, van Dorsselaer, A, Gaertig, J, Janke, C

Cell 2009
19531357 TTLL3 Is a tubulin glycine ligase that regulates the assembly of cilia

Wloga, D, Webster, DM, Rogowski, K, Bré, MH, Levilliers, N, Jerka-Dziadosz, M, Janke, C, Dougan, ST, Gaertig, J

Dev. Cell 2009
18331838 TTLL10 is a protein polyglycylase that can modify nucleosome assembly protein 1

Ikegami, K, Horigome, D, Mukai, M, Livnat, I, Macgregor, GR, Setou, M

FEBS Lett. 2008
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Catalyst Activity
Catalyst Activity
Title
protein-glycine ligase activity of TTLL3,TTLL8,TTLL10 [cytosol]
Physical Entity
Activity
Orthologous Events
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