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.
Gaertig, J, Webster, DM, Jerka-Dziadosz, M, Bré, MH, Levilliers, N, Rogowski, K, Janke, C, Dougan, ST, Wloga, D
Gaertig, J, Thomas, D, Bré, MH, Levilliers, N, Strub, JM, van Dorsselaer, A, Rogowski, K, Janke, C, van Dijk, J, Wloga, D, Juge, F
Mukai, M, Setou, M, Horigome, D, Livnat, I, Macgregor, GR, Ikegami, K
protein-glycine ligase activity of TTLL3,TTLL8,TTLL10 [cytosol]
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