Absence of 7-acetyl taxol binding to unassembled brain tubulin

• Published in: FEBS letters Vol. 227; no. 2; pp. 96 - 98
• Main Authors: Takoudju, Martin, Wright, Michel, Chenu, Jacques, Guéritte-Voegelein, Françoise, Guénard, Daniel
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 25.01.1988; Elsevier
• Subjects: 7-acetyl taxol; Ac-taxol; Alkaloids - metabolism; Animals; Biological and medical sciences; brain; Brain - metabolism; Cell structures and functions; Cytoskeleton, cytoplasm. Intracellular movements; Dialysis; dimethyl sulfoxide; Equilibrium dialysis; Fundamental and applied biological sciences. Psychology; Kinetics; Me2SO; Microtubule; Microtubules - metabolism; Molecular and cellular biology; Paclitaxel - analogs & derivatives; Protein Binding; Sheep; Taxoids; Taxol; Tritium; Tubulin; Tubulin - metabolism; Ac-taxol; Tubulin; Microtubule; Taxol; Me 2SO; Equilibrium dialysis; Vertebrata; Mammalia; Animal; Central nervous system; Cytoskeleton; Molecular interaction; Sheep; Artiodactyla; Ungulata
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(88)80875-5

The effect of taxol on microtubule proteins at 0°C is controversial. In order to determine if taxol is unable to bind to unassembled tubulin, as has been hypothesized, the binding of [ 3H]acetyl taxol has been studied using equilibrium microdialysis. Ac-taxol bound to microtubules at 37°C and the binding remained stable when the temperature was lowered to 0°C. Ac-taxol bound also at 0°C to microtubules stabilized with rhazinilam. In contrast, there was no binding of Ac-taxol to unassembled tubulin, either free tubulin at 0°C or tubulin, complexed with several microtubule poisons, at 0 and 37°C.