Polyglycylation

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This is a form of post translational 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].


[edit] References

  1. ^ 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, 1688-1691 ( http://www.sciencemag.org/cgi/content/abstract/266/5191/1688 )
  2. ^ Asok Banerjee Coordination of Posttranslational Modifications of Bovine Brain alpha -Tubulin. POLYGLYCYLATION OF Delta 2 TUBULIN J. Biol. Chem. 277: 46140-46144 ( http://www.jbc.org/cgi/content/full/277/48/46140 )


Protein primary structure and posttranslational modifications
General: Protein biosynthesis | Peptide bond | Proteolysis | Racemization | N-O acyl shift
N-terminus: Acetylation | Formylation | Myristoylation | 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 | deamination and oxidation to aldehyde| O-glycosylation | imine formation | glycation | carbamylation
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→
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