Two microtubule-associated proteins, tau and the high molecular weight microtubule-associated protein 2 (MAP 2), were purified from rat brain microtubules. Addition of either protein to pure tubulin caused microtubule assembly. In the presence of tau and 10 microM vinblastine, tubulin aggregated into spiral structures. If tau was absent, or replaced by MAP 2, little aggregation occurred in the presence of vinblastine. Thus, vinblastine may be a useful probe in elucidating the individual roles of tau and MAP 2 in microtubule assembly.
Article| June 01 1981
Effect of tau on the vinblastine-induced aggregation of tubulin.
R F Ludueña
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1981) 89 (3): 680–683.
R F Ludueña, A Fellous, J Francon, J Nunez, L McManus; Effect of tau on the vinblastine-induced aggregation of tubulin.. J Cell Biol 1 June 1981; 89 (3): 680–683. doi: https://doi.org/10.1083/jcb.89.3.680
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