Manso-Martínez R, Palomares R, Pariente F
Arch Biochem Biophys. 1984 Nov 15;235(1):196-203. doi: 10.1016/0003-9861(84)90268-6.
Microtubules assembled in vitro with ATP were depolymerized by the addition of cyclic AMP, which correlates with a stimulation of the endogeneous phosphorylation reaction. When assembled with GTP, however, microtubules were only sensitive to cyclic AMP when ATP was present. This nucleoside triphosphate induced the disassembly of microtubules in a concentration-dependent, cyclic nucleotide-stimulated manner. Since UTP, CTP and the nonhydrolyzable ATP analog adenosine-5'-(beta, gamma-methylene)triphosphate were without comparable effect, it was assumed that phosphorylation of the microtubule-associated proteins may represent a physiological mechanism by which microtubules in the living cell respond to external stimuli.
在体外与三磷酸腺苷（ATP）组装的微管，通过添加环磷酸腺苷（cAMP）而解聚，这与内源性磷酸化反应的刺激相关。然而，当与三磷酸鸟苷（GTP）组装时，只有在存在ATP的情况下微管才对环磷酸腺苷敏感。这种核苷三磷酸以浓度依赖性、环核苷酸刺激的方式诱导微管解聚。由于三磷酸尿苷（UTP）、三磷酸胞苷（CTP）以及不可水解的ATP类似物腺苷-5'-（β，γ-亚甲基）三磷酸没有类似作用，因此推测微管相关蛋白的磷酸化可能代表一种生理机制，通过该机制活细胞中的微管对外界刺激作出反应。
