Tubulin dynamics during the cytoplasmic cohesiveness cycle in artificially activated sea urchin eggs.
Tubulin dynamics during the cytoplasmic cohesiveness cycle in artificially activated sea urchin eggs.
复制标题
人工激活的海胆卵细胞质内聚周期中的微管蛋白动力学。
DOI：
10.1016/0014-4827(83)90353-1
复制
发表时间：
1983
影响因子：
3.7
通讯作者：
J. Pudles
中科院分区：
文献类型：
--
作者：
G. Coffe;G. Foucault;M. Raymond;J. Pudles
沉降研究和[3 H]秋水仙素结合试验表明，细胞质的凝聚力周期和微管蛋白的组织inParacentrotus lividuseggs激活2.5 mM普鲁卡因的变化之间的关系。相同量的微管蛋白（总卵微管蛋白的20- 25%）参与这些循环过程，并似乎经历聚合和解聚循环。电子显微镜研究表明，在这些细胞质内聚性周期中形成的微管是在一个微粒的形式，这是在低速沉降。在细胞松弛素B（CB）的存在下进行的活化实验表明，在细胞质的凝聚力的增加大大减少，而微管蛋白聚合和解聚周期和原核中心不受影响。虽然微管蛋白或肌动蛋白聚合可以独立地触发普鲁卡因激活的鸡蛋，细胞质内聚性的增加需要这两种蛋白质的聚合。然而，细胞质内聚性周期似乎受到微管蛋白聚合和解聚周期的调节。
Sedimentation studies and [3H]colchicine-binding assays have demonstrated a relationship between the cytoplasmic cohesiveness cycles and the changes in tubulin organization inParacentrotus lividuseggs activated by 2.5 mM procaine. The same amount of tubulin (20–25 % of the total egg tubulin) is involved in these cyclic process and appears to undergo polymerization and depolymerization cycles. Electron microscopy studies reveal that the microtubules formed during these cytoplasmic cohesiveness cycles are under a particulate form which is sedimentable at low speed. Activation experiments carried out in the presence of cytochalasin B (CB) show that the increase in the cytoplasmic cohesiveness is highly reduced while tubulin polymerization and depolymerization cycles and pronuclear centration are not affected. Although tubulin or actin polymerization can be independently triggered in procaine-activated eggs, the increase in cytoplasmic cohesiveness requires the polymerization of both proteins. However, the cytoplasmic cohesiveness cycles appear to be regulated by tubulin polymerization and depolymerization cycles.
海胆 Lytechinus variegatus 人工激活卵中微管的结构。
影响因子：
3.7
作者：
Bestor,TH;Schatten,G
通讯作者：
Schatten,G
影响因子：
--
作者：
OTTO, JJ;KANE, RE;BRYAN, J
通讯作者：
BRYAN, J
影响因子：
2.5
作者：
Redel, Bethany K.;Brown, Alana N.;Prather, Randall S.
通讯作者：
Prather, Randall S.