|Title||Cryo-electron tomography structure of Arp2/3 complex in cells reveals new insights into the branch junction.|
|Journal, issue, pages||Nat Commun, Vol. 11, Issue 1, Page 6437, Year 2020|
|Publish date||Dec 22, 2020|
|Authors||Florian Fäßler / Georgi Dimchev / Victor-Valentin Hodirnau / William Wan / Florian K M Schur /|
|PubMed Abstract||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 ...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 Å 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.|
|External links||Nat Commun / PubMed:33353942 / PubMed Central|
|Methods||EM (subtomogram averaging) / EM (tomography)|
EMDB-11869: Structure of the actin filament Arp2/3 complex branch junction in cells
|Keywords||Actin Cytoskeleton / Actin-Related Protein 2-3 Complex / Animals / Electron Microscope Tomography / Fibroblasts / Mice / Models, Molecular / NIH 3T3 Cells / Protein Conformation / Pseudopodia / STRUCTURAL PROTEIN / Actin / Arp2-3 complex / Cytoskeleton|
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