Polyglycylation
Polyglycylation is a form of posttranslational modification of glutamate residues of the carboxyl-terminal region tubulin in certain microtubules (e.g., axonemal) originally discovered in Paramecium,[1] and later shown in mammalian neurons as well.[2]
See also
- Polyglutamylation
References
- ^ Redeker V, Levilliers N, Schmitter JM, Le Caer JP, Rossier J, Adoutte A, Bré MH (1994). "Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules". Science. 266 (5191): 1688–1691. 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): 46140–46144. doi:10.1074/jbc.M208065200. PMID 12356754.
- v
- t
- e
Protein primary structure and posttranslational modifications
- Peptide bond
- Protein biosynthesis
- Proteolysis
- Racemization
- N–O acyl shift
- Acetylation
- Carbamylation
- Formylation
- Glycation
- Methylation
- Myristoylation (Gly)
- Amidation
- Glycosyl phosphatidylinositol (GPI)
- O-methylation
- Detyrosination
| Cysteine–Cysteine | |
|---|---|
| Methionine–Hydroxylysine | |
| Lysine–Tyrosine |
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| Tryptophan–Tryptophan |
| Serine–Tyrosine–Glycine |
|
|---|---|
| Histidine–Tyrosine–Glycine |
|
| Alanine–Serine–Glycine |
| Allysine–Allysine–Allysine–Lysine |
|---|
