Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction

被引:56
作者
Fassler, Florian [1 ]
Dimchev, Georgi [1 ]
Hodirnau, Victor-Valentin [1 ]
Wan, William [2 ,3 ]
Schur, Florian K. M. [1 ]
机构
[1] IST Austria, Klosterneuburg, Austria
[2] Vanderbilt Univ, Dept Biochem, Nashville, TN 37232 USA
[3] Vanderbilt Univ, Ctr Struct Biol, 221 Kirkland Hall, Nashville, TN 37235 USA
基金
奥地利科学基金会;
关键词
ACTIN; NUCLEATION; VISUALIZATION; MODEL; ELECTROSTATICS; IMPLEMENTATION; LAMELLIPODIA; ORGANIZATION; NETWORKS; BINDING;
D O I
10.1038/s41467-020-20286-x
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
The actin-related protein (Arp)2/3 complex nucleates branched actin filament networks pivotal for cell migration, endocytosis and pathogen infection. Its activation is tightly regulated and involves complex structural rearrangements and actin filament binding, which are yet to be understood. Here, we report a 9.0 angstrom resolution structure of the actin filament Arp2/3 complex branch junction in cells using cryo-electron tomography and subtomogram averaging. This allows us to generate an accurate model of the active Arp2/3 complex in the branch junction and its interaction with actin filaments. Notably, our model reveals a previously undescribed set of interactions of the Arp2/3 complex with the mother filament, significantly different to the previous branch junction model. Our structure also indicates a central role for the ArpC3 subunit in stabilizing the active conformation. The actin-related protein (Arp)2/3 complex nucleates branched actin filament networks pivotal for cell migration, endocytosis and pathogen infection. Here, authors report a 9.0 angstrom resolution structure of the actin filament Arp2/3 complex branch junction in cells using cryo-electron tomography and subtomogram averaging.
引用
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页数:10
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