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- W2007016724 abstract "Western blot analyses of total assembled microtubule fractions from NB2a/d1 neuroblastoma cells demonstrated that these cells are capable of post-translationally modifying alpha-tubulin by acetylation and detyrosination. Immunocytochemical analyses of NB2a/d1 cells differentiated with dbcAMP which had been processed under microtubule-stabilizing conditions demonstrated that all forms of alpha-tubulin were present throughout perikarya and neurites. By contrast, extraction of cells with Triton X-100 revealed a regional concentration of acetylated and detyrosinated alpha-tubulin subunits within axonal neurites, detectable in some cells after 3 days of differentiation and in nearly all cells after 7 days. Resistance of neurites to retraction following colchicine-treatment developed at a similar rate; furthermore, colchicine-resistant neurites contained intense acetylated alpha-tubulin immunoreactivity. We conclude that NB2a/d1 cells are capable of acetylating and detyrosinating alpha-tubulin subunits and that selective post-translational modification of alpha-tubulin subunits may be related to neuritic maturation." @default.
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- W2007016724 date "1990-02-01" @default.
- W2007016724 modified "2023-09-27" @default.
- W2007016724 title "Post-translational modification of α-tubulin by acetylation and detyrosination in NB2a/d1 neuroblastoma cells" @default.
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- W2007016724 doi "https://doi.org/10.1016/0165-3806(90)90276-5" @default.
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