Posttranslational glutamylation of alpha-tubulin.
The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of alpha-tubulin can be posttranslationally labeled after incubation of cells with [3H]acetate or [3H]glutamate. Peptides carrying the radioactive moiety were purified by high-performance liquid chromatography. Amino acid analysis, Edman degradation sequencing, and mass spectrometric analysis of these peptides led to the characterization of a posttranslational modification consisting of the successive addition of glutamyl units on the gamma-carboxyl group of a glutamate residue (Glu445). This modification, localized within a region of alpha-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.
Eddé
B
B
Laboratoire de Biochimie Cellulaire, Collège de France, Paris.
Rossier
J
J
Le Caer
J P
JP
Desbruyères
E
E
Gros
F
F
Denoulet
P
P
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001921:Brain / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D005971:Glutamates / Q000378:metabolism*; D018698:Glutamic Acid; D013058:Mass Spectrometry; D051379:Mice; D009474:Neurons / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011499:Protein Processing, Post-Translational; D014404:Tubulin / Q000378:metabolism*
D000596:Amino Acids; D005971:Glutamates; D010446:Peptide Fragments; D014404:Tubulin; D018698:Glutamic Acid