Posttranslational modifications of alpha-tubulin: acetylated and detyrosinated forms in axons of rat cerebellum.
The distribution of acetylated alpha-tubulin in rat cerebellum was examined and compared with that of total alpha-tubulin and tyrosinated alpha-tubulin. From immunoperoxidase-stained vibratome sections of rat cerebellum it was found that acetylated alpha-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 alpha-tubulin, indicating that parallel fibers contain alpha-tubulin that is acetylated and detyrosinated. Axonal microtubules are known to be highly stable and the distribution of acetylated alpha-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.
Cambray-Deakin
M A
MA
Burgoyne
R D
RD
D000107:Acetylation; D000818:Animals; D001369:Axons / Q000032:analysis*; D001923:Brain Chemistry; D002478:Cells, Cultured; D002531:Cerebellum / Q000032:analysis*; D003712:Dendrites / Q000032:analysis; D007124:Immunoenzyme Techniques; D009457:Neuroglia / Q000032:analysis; D011499:Protein Processing, Post-Translational; D011689:Purkinje Cells / Q000032:analysis; D051381:Rats; D014404:Tubulin / Q000032:analysis / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism
D014404:Tubulin; D014443:Tyrosine