An actin nucleation mechanism mediated by Bni1 and profilin

被引:384
作者
Sagot, I
Rodal, AA
Moseley, J
Goode, BL
Pellman, D
机构
[1] Harvard Univ, Sch Med, Dept Pediat Oncol, Dana Farber Canc Inst,Childrens Hosp, Boston, MA 02115 USA
[2] Harvard Univ, Sch Med, Dept Pediat Hematol, Childrens Hosp, Boston, MA 02115 USA
[3] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[4] Brandeis Univ, Rosenstiel Med Ctr, Dept Biol, Waltham, MA 02454 USA
关键词
D O I
10.1038/ncb834
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Formins are required for cell polarization and cytokinesis, but do not have a defined biochemical activity. In Saccharomyces cerevisiae, formins and the actin-monomer-binding protein profilin are specifically required to assemble linear actin structures called 'actin cables'. These structures seem to be assembled independently of the Arp2/3 complex, the only well characterized cellular mediator of actin nucleation. Here, an activated yeast formin was purified and found to promote the nucleation of actin filaments in vitro. Formin-dependent actin nucleation was stimulated by profilin. Thus, formin and profilin mediate actin nucleation by an Arp2/3-independent mechanism. These findings suggest that distinct actin nucleation mechanisms may underlie the assembly of different actin cytoskeletal structures.
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收藏
页码:626 / 631
页数:6
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