The C terminus of -tubulin regulates vinblastine-induced tubulin polymerization
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چکیده
منابع مشابه
The C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization.
Oligoanions such as sodium triphosphate or GTP prevent and/or reverse vinblastine-induced polymerization of tubulin. We now show that the anions of glutamate-rich extreme C termini of tubulin are similarly involved in the regulation of the vinblastine effect. Cleavage of the C termini by limited proteolysis with subtilisin enhances vinblastine-induced tubulin polymerization and abolishes the an...
متن کاملIn vitro vinblastine-induced tubulin paracrystals.
Purified calf brain tubulin has been induced to self-aggregate in vitro into paracrystalline structures by the anti-cancer drug vinblastine. The size, shape, optical birefringence, and drug stoichiometry of these tubulin-vinblastine paracrystals are similar to those of paracrystals formed in vivo. Similar structures can be formed with vincristine and desacetylvinblastine, but not with colchicin...
متن کاملEffect of tau on the vinblastine-induced aggregation of tubulin
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 ...
متن کاملAb Initio Study of Vinblastine-Tubulin Anticancer Complex
Vinblastine is an important anticancer agent known to diminish microtubule assembly. Ab initio calculations are applied to examine the structural properties and different energies of vinblastine-tubulin complex in different dielectric constants and temperatures. The aims of this work are discovery the best optimized structure and thermodynamic properties of vinblastine-tubulin complex ...
متن کاملMaytansine binding to the vinblastine sites of tubulin.
Tubulin possesses two distinct binding sites for vinblastine; one of high affinity (Ka = 6.2 X 106M” ) occupancy of which prevents polymerization of tubulin and a second, lower affinity site (K, = 8 X 104M”) occupancy of which correlates with the aggregating effects of the alkaloid on tubulin [l]. The recent report [2] that maytansine, a new antitumor agent of plant origin [3,4] , was a potent ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1998
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.95.8.4253