Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
复制标题
细胞切拉斯蛋白的作用机理：证据与肌动蛋白丝结束。
DOI：
10.1083/jcb.88.3.487
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发表时间：
1981-03
影响因子：
7.8
通讯作者：
Spudich, J A
中科院分区：
文献类型：
--
作者：
Brown, S S;Spudich, J A
为了验证细胞松弛素通过与微丝末端结合来抑制肌动蛋白组装的想法，我们设计了一种新的细胞松弛蛋白结合方法，其中微丝末端的数量可以独立于肌动蛋白总浓度而变化。肌动蛋白与聚赖氨酸包裹的聚苯乙烯珠子反应，形成丝状末端(Brown和Spudich，1979，J.Cell Biol)。80：499-504)，然后与[~3H]细胞松弛素B反应。我们发现，细胞松弛素B在肌动蛋白存在的情况下与珠子结合，并且细胞松弛素B结合位点的数目可以作为丝状末端数目的函数而不受总肌动蛋白浓度的影响。
To test the idea that cytochalasin retards actin assembly by binding to filament ends, we have designed a new assay for cytochalasin binding in which the number of filament ends can be varied independently of the total actin concentration. Actin is reacted with polylysine-coated polystyrene beads to make filament ends (Brown and Spudich, 1979, J. Cell Biol. 80:499-504) and then reacted with [3H]cytochalasin B. We have found that cytochalasin B binds to beads in the presence of actin, and that the number of cytochalasin B binding sites can be varied as a function of the number of filament ends independent of the total actin concentration by varying the bead concentration.