Role of formins in actin assembly: Nucleation and barbed-end association

被引:559
作者
Pruyne, D
Evangelista, M
Yang, CS
Bi, EF
Zigmond, S
Bretscher, A [1 ]
Boone, C
机构
[1] Queens Univ, Dept Biol, Kingston, ON K7L 3N6, Canada
[2] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA
[3] Univ Penn, Dept Biol, Philadelphia, PA 19104 USA
[4] Univ Penn, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA
[5] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada
[6] Univ Toronto, Dept Mol & Med Genet, Toronto, ON M5G 1L6, Canada
关键词
D O I
10.1126/science.1072309
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Nucleation of branched actin laments by the Arp2/3 complex is a conserved process in eukaryotic cells, yet the source of unbranched actin laments has remained obscure. In yeast, formins stimulate assembly of actin cables independently of Arp2/3. Here, the conserved core of formin homology domains 1 and 2 of Bni1p (Bni1pFH1FH2) was found to nucleate unbranched actin laments in vitro. Bni1pFH2 provided the minimal region sufficient for nucleation. Unique among actin nucleators, Bni1pFH1FH2 remained associated with the growing barbed ends of laments. This combination of properties suggests a direct role for formins in regulating nucleation and polarization of unbranched filamentous actin structures.
引用
收藏
页码:612 / 615
页数:4
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