THE MULTIPLE PHOSPHORYLATION OF THE MICROTUBULE-ASSOCIATED PROTEIN MAP2 CONTROLS THE MAP2 - TUBULIN INTERACTION
THE MULTIPLE PHOSPHORYLATION OF THE MICROTUBULE-ASSOCIATED PROTEIN MAP2 CONTROLS THE MAP2 - TUBULIN INTERACTION
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DOI：
10.1111/j.1432-1033.1984.tb08236.x
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发表时间：
1984-01-01
期刊：
影响因子：
--
通讯作者：
CHAPMAN, R
中科院分区：
文献类型：
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作者：
BURNS, RG;ISLAM, K;CHAPMAN, R
与共纯化cAMP非依赖性蛋白激酶的鸡微管相关蛋白MAP 2的预磷酸化降低了MAP 2对紫杉醇稳定的微管的亲和力，增加了微管聚合的解离速率常数，每一个都依赖于磷酸化水平，但对缔合速率常数没有影响。微管组装对磷酸化的动力学没有影响，而预组装微管的磷酸化导致其以与磷酸化的初始速率成比例的速率立即解聚。MAP 2的磷酸化调节可能在体内调节微管长度。
Pre-phosphorylation of chicken microtubule-associated protein MAP2 with the co-purifying cAMP-independent protein kinase decreases the affinity of MAP2 for taxol-stabilized microtubules, increases the dissociation rate constant for microtubule polymerization, each of which is dependent on the level of phosphorylation, but has no effect on the association rate constant. Microtubule assembly has no effect on the kinetics of phosphorylation whereas phosphorylation of pre-assembled microtubules causes their immediate depolymerization at a rate which is proportional to the initial rate of phosphorylation. The modulated phosphorylation of MAP2 may regulate microtubule length in vivo.