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Polyglycylation

Polyglycylation is a form of posttranslational modification of glutamate residues of the carboxyl-terminal region tubulin in certain microtubules (eg axonemal) originally discovered in paramecium^[1], and later shown in mammalian neurons as well^[2].

References

^ Redeker, V., Levilliers, N., Schmitter, J.M., Le Caer, J.P., Rossier, J., Adoutte, A., and Bré, M.H. (1994). "Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules". Science 266 (5191): 1688–91. doi:10.1126/science.7992051. PMID 7992051.
^ Banerjee Asok (2002). "Coordination of posttranslational modifications of bovine brain alpha-tubulin. Polyglycylation of delta2 tubulin". J. Biol. Chem. 277 (48): 46140–4. doi:10.1074/jbc.M208065200. PMID 12356754.

v • d • e Protein primary structure and posttranslational modifications
General	Protein biosynthesis \| Peptide bond \| Proteolysis \| Racemization \| N-O acyl shift
N-terminus	Acetylation \| Formylation \| Pyroglutamate \| Methylation \| Glycation \| Myristoylation (Gly) \| carbamylation
C-terminus	Amidation \| Glycosyl phosphatidylinositol (GPI) \| O-methylation \| Glypiation \| Ubiquitination \| Sumoylation
Lysine	Methylation \| Acetylation \| Acylation \| Hydroxylation \| Ubiquitination \| SUMOylation \| Desmosine \| ADP-ribosylation \| Deamination and Oxidation to aldehyde
Cysteine	Disulfide bond \| Prenylation \| Palmitoylation
Serine/Threonine	Phosphorylation \| Glycosylation
Tyrosine	Phosphorylation \| Sulfation \| Porphyrin ring linkage \| Flavin linkage \| GFP prosthetic group (Thr-Tyr-Gly sequence) formation \| Lysine tyrosine quinone (LTQ) formation \| Topaquinone (TPQ) formation
Asparagine	Deamidation \| Glycosylation
Aspartate	Succinimide formation
Glutamine	Transglutamination
Glutamate	Carboxylation \| Polyglutamylation \| Polyglycylation
Arginine	Citrullination \| Methylation
Proline	Hydroxylation
←Amino acids Secondary structure→