GCAP39, A CALCIUM ION- AND POLYPHOSPHOINOSITIDE-REGULATED ACTIN CAPPING PROTEIN
GCAP39, A CALCIUM ION- AND POLYPHOSPHOINOSITIDE-REGULATED ACTIN CAPPING PROTEIN
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DOI：
10.1126/science.2255912
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发表时间：
1990-12-07
期刊：
影响因子：
56.9
通讯作者：
YIN, HL
中科院分区：
文献类型：
--
作者：
YU, FX;JOHNSTON, PA;YIN, HL
肌动蛋白丝的聚合与生长、运动和细胞分裂有关。研究表明，肌动蛋白的聚合受凝溶胶蛋白的控制，凝溶胶蛋白与肌动蛋白的相互作用受钙离子（Ca ~（2+））的激活和膜聚磷酸肌醇（PPI）的抑制。一个较小的钙和PPI调节蛋白，gCap 39，它有49%的序列同一性与凝溶胶蛋白，已被确定通过cDNA克隆和蛋白纯化。与凝溶胶蛋白一样，gCap 39与肌动蛋白丝的快速生长（+）端结合。然而，gCap 39不切断肌动蛋白丝，可以响应Ca 2+和PPI瞬变独立，在凝溶胶蛋白是无效的条件下。gCap 39与凝溶胶蛋白的共存应该允许在细胞的前缘精确调节肌动蛋白组装。
The polymerization of actin filaments is involved in growth, movement, and cell division. It has been shown that actin polymerization is controlled by gelsolin, whose interactions with actin are activated by calcium ion (Ca2+) and inhibited by membrane polyphosphoinositides (PPI). A smaller Ca2+- and PPI-regulated protein, gCap39, which has 49% sequence identity with gelsolin, has been identified by cDNA cloning and protein purification. Like gelsolin, gCap39 binds to the fast-growing (+) end of actin filaments. However, gCap39 does not sever actin filaments and can respond to Ca2+ and PPI transients independently, under conditions in which gelsolin is ineffective. The coexistence of gCap39 with gelsolin should allow precise regulation of actin assembly at the leading edge of the cell.