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First published online September 12, 2003

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A tubulin polyglutamylase subunit

Polyglutamylation of tubulin is common at centrioles, basal bodies and axonemes and characteristic of most neuronal microtubules. This modification is implicated in control of centriole stability, axoneme beating and neuronal differentiation, but the enzyme responsible has eluded researchers. Bernard Eddé and co-workers have now identified and characterized one of its subunits, PGs1 (see p. 4181). Starting with a partially purified preparation from mouse brain, the authors use immunoprecipitation to show that the polyglutamylase comprises three polypeptides: p32 (PGs1), p50 and p80. They then demonstrate by mass spectrometry and database searches that the PGs1 subunit is encoded by GTRGEO22, a gene whose mutation is associated with formation of abnormal spermatid flagella and male sterility. Eddé and co-workers confirm that PGs1 is indeed a component of the enzyme by showing that a monoclonal antibody specific for the protein pulls down polyglutamylase activity. Immunofluorescence studies using this antibody indicate that PGs1 colocalizes with highly polyglutamylated structures, including centrosomes, basal bodies and neurite microtubules. Since PGs1 has no intrinsic enzymatic activity but continues to localize correctly when overexpressed, the authors suggest it acts as a targeting subunit for the polyglutamylase complex.

Related articles in JCS:

Characterisation of PGs1, a subunit of a protein complex co-purifying with tubulin polyglutamylase

Catherine Regnard, Didier Fesquet, Carsten Janke, Dominique Boucher, Elisabeth Desbruyères, Annette Koulakoff, Christine Insina, Pierre Travo, and Bernard Eddé
JCS 2003 116: 4181-4190. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content