期刊
CURRENT BIOLOGY
卷 13, 期 20, 页码 1820-1823出版社
CELL PRESS
DOI: 10.1016/j.cub.2003.09.057
关键词
-
资金
- NIAID NIH HHS [AI19883] Funding Source: Medline
Formins, characterized by formin homology domains FH1 and FH2, are required to assemble certain F-actin structures including actin cables, stress fibers, and the contractile ring. FH1FH2 in a recombinant fragment from a yeast formin (Bni1p) nucleates actin filaments in vitro [1, 2]. It also binds to the filament barbed end where it appears to act as a leaky capper, slowing both polymerization and depolymerization by similar to50% [3]. We now find that FH1FH2 competes with tight capping proteins (including gelsolin and heterodimeric capping protein) for the barbed end. We also find that FH1FH2 forms a tetramer. The observation that this formin protects an end from capping but still allows elongation confirms that it is a leaky capper. This is significant because a nucleator that protects a new barbed end from tight cappers will increase the duration of elongation and thus the total amount of F-actin. The ability of FH1FH2 to dimerize probably allows the formin to walk processively with the barbed end as the filament elongates.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据