Posttranslational modifications of α-tubulin: Acetylated and detyrosinated forms in axons of rat cerebellum

Abstract

The distribution of acetylated α-tubulin in rat cerebellum was examined and compared with that of total α-tubulin and tyrosinated α-tubulin. From immunoperoxidase-stained vibratome sections of rat cerebellum it was found that acetylated α-tubulin, detectable with monoclonal 6-11B-1, was preferentially enriched in axons compared with dendrites. Parallel fiber axons, in particular, were labeled with 6-11B-1 yet unstained by an antibody recognizing tyrosinated α-tubulin, indicating that parallel fibers contain α-tubulin that is acetylated and detyrosinated. Axonal microtubules are known to be highly stable and the distribution of acetylated α-tubulin in other classes of stable microtubules suggests that acetylation and possibly detyrosination may play a role in the maintenance of stable populations of microtubules.