Control of the assembly of ATP- and ADP-actin by formins and profilin

被引:431
|
作者
Kovar, DR
Harris, ES
Mahaffy, R
Higgs, HN
Pollard, TD [1 ]
机构
[1] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[2] Yale Univ, Dept Cell Biol, New Haven, CT 06520 USA
[3] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[4] Dartmouth Coll Sch Med, Dept Biochem, Hanover, NH 03755 USA
关键词
D O I
10.1016/j.cell.2005.11.038
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Formin proteins nucleate actin filaments, remaining processively associated with the fast-growing barbed ends. Although formins possess common features, the diversity of functions and biochemical activities raised the possibility that formins differ in fundamental ways. Further, a recent study suggested that profilin and ATP hydrolysis are both required for processive elongation mediated by the formin mDia1. We used total internal reflection fluorescence microscopy to observe directly individual actin filament polymerization in the presence of two mammalian formins (mDial1 and mDia2) and two yeast formins (Bni1p and Cdc12p). We show that these diverse formins have the same basic properties: movement is processive in the absence or presence of profilin; profilin accelerates elongation; and actin ATP hydrolysis is not required for processivity. These results suggest that diverse formins are mechanistically similar, but the rates of particular assembly steps vary.
引用
收藏
页码:423 / 435
页数:13
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