Peering deeply inside the branch.

Peering deeply inside the branch.
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DOI:
10.1083/jcb.200802062
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发表时间:
2008-03-10
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Bear JE
Bear JE
中科院分区:
其他
文献类型:
--
作者:
Cai L;Bear JE

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肌动蛋白相关蛋白2/3(Arp2/3)的故事十多年来一直吸引着细胞骨架界的注意力。这种复合体不仅可以形成新的肌动蛋白细丝,还可以将它们锚定在树突网络中,这种网络在许多细胞环境中都有使用,如板脂突起、内体火箭和病原体的运动。这个谜题的一个关键部分是Arp2/3-肌动蛋白分支的详细结构。使用电子断层扫描和计算对接,Rouiller等人。(Rouiller,I.,X.-P.Xu,K.J.Amann,C.Egile,S.Nickell,D.Nicstro,R.Li,T.D.Pollard,N.Volkmann,D.Hanein.2008年。J.细胞生物学。180:887-895)呈现了Arp2/3复合体介导的肌动蛋白分支优雅而耐人寻味的结构。
The actin-related protein 2/3 (Arp2/3) story has captivated the cytoskeleton community for over a decade. Not only does this complex nucleate new actin filaments, but it also anchors them into a dendritic meshwork that is used in many cellular contexts such as lamellipodial protrusion, endosome rocketing, and the movement of pathogens. One key piece of this puzzle that has been missing is a detailed structure of the Arp2/3-actin branch. Using electron tomography and computational docking, Rouiller et al. (Rouiller, I., X.-P. Xu, K.J. Amann, C. Egile, S. Nickell, D. Nicastro, R. Li, T.D. Pollard, N. Volkmann, and D. Hanein. 2008. J. Cell Biol. 180:887–895) present an elegant and intriguing structure of the Arp2/3 complex–mediated actin branch.
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