Posttranslational Glutamylation of α-tubulin

Abstract

The high degree of tubulin heterogeneity in neurons is controlled mainly at the posttranslational level. Several variants of α-tubulin can be posttranslationally labeled after incubation of cells with [ 3 H]acetate or [ 3 H]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 γ-carboxyl group of a glutamate residue (Glu 445 ). This modification, localized within a region of α-tubulin that is important in the interactions of tubulin with microtubule-associated proteins and calcium, could play a role in regulating microtubule dynamics.

Keywords

Edman degradationTubulinMicrotubuleResidue (chemistry)MoietyBiochemistryAmino acidChemistryPeptide sequenceBiologyStereochemistryCell biology

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Publication Info

Year: 1990
Type: article
Volume: 247
Issue: 4938
Pages: 83-85
Citations: 539
Access: Closed

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APA Style

                            
                                
                                    Bernard Eddé, 
                                
                                    Jean Rossier, 
                                
                                    Jean‐Pierre Le Caër
                                
                                et al.
                            
                            (1990). 
                            Posttranslational Glutamylation of α-tubulin. 
                            Science
                            , 247
                            (4938)
                            , 83-85.
                            https://doi.org/10.1126/science.1967194
                        

Identifiers

DOI: 10.1126/science.1967194