胶溶蛋白
肌动蛋白
肌动蛋白结合蛋白
细胞生物学
肌动蛋白重塑
神经元肌动蛋白重塑
MDia1公司
化学
肌动蛋白细胞骨架
生物
生物物理学
细胞骨架
生物化学
细胞
作者
Fu-Xin Yu,Paul A. Johnston,Thomas C. Südhof,Helen L. Yin
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1990-12-07
卷期号:250 (4986): 1413-1415
被引量:194
标识
DOI:10.1126/science.2255912
摘要
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.
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