Science. 1990 Jan 5;247(4938):83-5.

Posttranslational glutamylation of alpha-tubulin.

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

Source

Laboratoire de Biochimie Cellulaire, Collège de France, Paris.

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.

PMID:: 1967194; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances

Publication Types

Research Support, Non-U.S. Gov't

MeSH Terms

Substances

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

GLUTAMIC ACID HYDROCHLORIDE - HSDB

Supplemental Content

Related citations

A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity. [J Cell Biochem. 1991]
A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity.
Eddé B, Rossier J, Le Caer JP, Berwald-Netter Y, Koulakoff A, Gros F, Denoulet P. J Cell Biochem. 1991 Jun; 46(2):134-42.
Structure of the polyglutamyl side chain posttranslationally added to alpha-tubulin. [J Biol Chem. 1991]
Structure of the polyglutamyl side chain posttranslationally added to alpha-tubulin.
Redeker V, Le Caer JP, Rossier J, Promé JC. J Biol Chem. 1991 Dec 5; 266(34):23461-6.
Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: alpha 4 is glutamylated at two residues. [Biochemistry. 1998]
Posttranslational modifications of the C-terminus of alpha-tubulin in adult rat brain: alpha 4 is glutamylated at two residues.
Redeker V, Rossier J, Frankfurter A. Biochemistry. 1998 Oct 20; 37(42):14838-44.
Review Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins. [Methods Cell Biol. 2010]
Review Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins.
Redeker V. Methods Cell Biol. 2010; 95:77-103.
Review [Microtubules: functional polymorphisms of tubulin and associated proteins (structural and motor MAP's)]. [C R Seances Soc Biol Fil. 1996]
Review [Microtubules: functional polymorphisms of tubulin and associated proteins (structural and motor MAP's)].
Regnard C, Audebert S, Boucher D, Larcher JC, Eddé B, Denoulet P. C R Seances Soc Biol Fil. 1996; 190(2-3):255-68.

See reviews... See all...

Cited by 49 PubMed Central articles

The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized. [Mol Biol Cell. 2011]
The posttranslational modification of tubulin undergoes a switch from detyrosination to acetylation as epithelial cells become polarized.
Quinones GB, Danowski BA, Devaraj A, Singh V, Ligon LA. Mol Biol Cell. 2011 Apr; 22(7):1045-57. Epub 2011 Feb 9.
Synthesis of Peptides from α- and β-Tubulin Containing Glutamic Acid Side-Chain Linked Oligo-Glu with Defined Length. [Int J Pept. 2010]
Synthesis of Peptides from α- and β-Tubulin Containing Glutamic Acid Side-Chain Linked Oligo-Glu with Defined Length.
Tegge W, Bonafe CF, Teichmann A, Erck C. Int J Pept. 2010; 2010:189396. Epub 2010 Dec 15.
The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation. [Proc Natl Acad Sci U S A. 2010]
The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation.
Shida T, Cueva JG, Xu Z, Goodman MB, Nachury MV. Proc Natl Acad Sci U S A. 2010 Dec 14; 107(50):21517-22. Epub 2010 Nov 10.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Compound (MeSH Keyword)
PubChem chemical compound records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Substance (MeSH Keyword)
PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

Posttranslational glutamylation of alpha-tubulin.
Posttranslational glutamylation of alpha-tubulin.
Science. 1990 Jan 5 ;247(4938):83-5.

PubMed
Frequencies of human influenza-specific antibody secreting cells or plasmablasts...
Frequencies of human influenza-specific antibody secreting cells or plasmablasts post vaccination from fresh and frozen peripheral blood mononuclear cells.
J Immunol Methods. 2009 Jan 1 ;340(1):42-7. Epub 2008 Nov 6 .

PubMed
Endogenous 4-1BB ligand plays a critical role in protection from influenza-induc...
Endogenous 4-1BB ligand plays a critical role in protection from influenza-induced disease.
J Immunol. 2009 Jan 15 ;182(2):934-47.

PubMed
Renal failure due to acute phosphate nephropathy.
Renal failure due to acute phosphate nephropathy.
Neth J Med. 2008 Nov ;66(10):438-41.

PubMed
Disruption of alpha-actinin-integrin interactions at focal adhesions renders ost...
Disruption of alpha-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis.
Am J Physiol Cell Physiol. 2006 Nov ;291(5):C909-21. Epub 2006 Jun 28 .

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Display Settings:

Send to: