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PMID: 1967194 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Posttranslational glutamylation of alpha-tubulin.

Science (New York, N.Y.) ·Vol. 247 ·No. 4938 ·1990-01-05 ·Pages 83-5

Eddé B, Rossier J, Le Caer JP, Desbruyères E, Gros F, Denoulet P

Abstract

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.

MeSH Terms
Amino Acids/analysis Animals Brain/metabolism Chromatography, High Pressure Liquid Glutamates/metabolism Glutamic Acid Mass Spectrometry Mice Neurons/metabolism Peptide Fragments/analysis Protein Processing, Post-Translational Tubulin/metabolism
Chemicals
Amino Acids Glutamates Peptide Fragments Tubulin Glutamic Acid
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Eddé B
Laboratoire de Biochimie Cellulaire, Collège de France, Paris.
Rossier J
Le Caer J P
Desbruyères E
Gros F
Denoulet P
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1990-01-05
Pages
83-5
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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